ID TAF6_HUMAN Reviewed; 677 AA. AC P49848; A4D2B2; A4D2B3; B4DT11; D6W5U2; Q6AI29; DT 01-OCT-1996, integrated into UniProtKB/Swiss-Prot. DT 01-OCT-1996, sequence version 1. DT 02-SEP-2026, entry version 230. DE RecName: Full=Transcription initiation factor TFIID subunit 6; DE AltName: Full=RNA polymerase II TBP-associated factor subunit E; DE AltName: Full=Transcription initiation factor TFIID 70 kDa subunit; DE Short=TAF(II)70; DE Short=TAFII-70; DE Short=TAFII70; DE AltName: Full=Transcription initiation factor TFIID 80 kDa subunit; DE Short=TAF(II)80; DE Short=TAFII-80; DE Short=TAFII80; GN Name=TAF6; Synonyms=TAF2E, TAFII70; OS Homo sapiens (Human). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia; OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae; OC Homo. OX NCBI_TaxID=9606; RN [1] RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1 AND 2), PROTEIN SEQUENCE OF 78-95 RP AND 501-521, AND INTERACTION WITH TBP AND TAF1. RC TISSUE=Cervix carcinoma; RX PubMed=8262073; DOI=10.1002/j.1460-2075.1993.tb06226.x; RA Weinzierl R.O., Ruppert S., Dynlacht B.D., Tanese N., Tjian R.; RT "Cloning and expression of Drosophila TAFII60 and human TAFII70 reveal RT conserved interactions with other subunits of TFIID."; RL EMBO J. 12:5303-5309(1993). RN [2] RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), PROTEIN SEQUENCE OF 78-103; RP 113-127; 368-383 AND 441-455, AND INTERACTION WITH TBP; TAF1; TAF9; TAF12; RP GTF2F1 AND GTF2E1. RC TISSUE=Placenta; RX PubMed=7667268; DOI=10.1073/pnas.92.18.8195; RA Hisatake K., Ohta T., Takada R., Guermah M., Horikoshi M., Nakatani Y., RA Roeder R.G.; RT "Evolutionary conservation of human TATA-binding-polypeptide-associated RT factors TAFII31 and TAFII80 and interactions of TAFII80 with other TAFs and RT with general transcription factors."; RL Proc. Natl. Acad. Sci. U.S.A. 92:8195-8199(1995). RN [3] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 3). RX PubMed=14702039; DOI=10.1038/ng1285; RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S., RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., RA Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., RA Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., RA Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., RA Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., RA Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., RA Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., RA Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., RA Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., RA Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., RA Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., RA Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., RA Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., RA Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., RA Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., RA Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., RA Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., RA Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., RA Isogai T., Sugano S.; RT "Complete sequencing and characterization of 21,243 full-length human RT cDNAs."; RL Nat. Genet. 36:40-45(2004). RN [4] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1). RC TISSUE=Brain cortex; RX PubMed=17974005; DOI=10.1186/1471-2164-8-399; RA Bechtel S., Rosenfelder H., Duda A., Schmidt C.P., Ernst U., RA Wellenreuther R., Mehrle A., Schuster C., Bahr A., Bloecker H., Heubner D., RA Hoerlein A., Michel G., Wedler H., Koehrer K., Ottenwaelder B., Poustka A., RA Wiemann S., Schupp I.; RT "The full-ORF clone resource of the German cDNA consortium."; RL BMC Genomics 8:399-399(2007). RN [5] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND VARIANT SER-36. RG NIEHS SNPs program; RL Submitted (SEP-2002) to the EMBL/GenBank/DDBJ databases. RN [6] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RX PubMed=12690205; DOI=10.1126/science.1083423; RA Scherer S.W., Cheung J., MacDonald J.R., Osborne L.R., Nakabayashi K., RA Herbrick J.-A., Carson A.R., Parker-Katiraee L., Skaug J., Khaja R., RA Zhang J., Hudek A.K., Li M., Haddad M., Duggan G.E., Fernandez B.A., RA Kanematsu E., Gentles S., Christopoulos C.C., Choufani S., Kwasnicka D., RA Zheng X.H., Lai Z., Nusskern D.R., Zhang Q., Gu Z., Lu F., Zeesman S., RA Nowaczyk M.J., Teshima I., Chitayat D., Shuman C., Weksberg R., RA Zackai E.H., Grebe T.A., Cox S.R., Kirkpatrick S.J., Rahman N., RA Friedman J.M., Heng H.H.Q., Pelicci P.G., Lo-Coco F., Belloni E., RA Shaffer L.G., Pober B., Morton C.C., Gusella J.F., Bruns G.A.P., Korf B.R., RA Quade B.J., Ligon A.H., Ferguson H., Higgins A.W., Leach N.T., RA Herrick S.R., Lemyre E., Farra C.G., Kim H.-G., Summers A.M., Gripp K.W., RA Roberts W., Szatmari P., Winsor E.J.T., Grzeschik K.-H., Teebi A., RA Minassian B.A., Kere J., Armengol L., Pujana M.A., Estivill X., RA Wilson M.D., Koop B.F., Tosi S., Moore G.E., Boright A.P., Zlotorynski E., RA Kerem B., Kroisel P.M., Petek E., Oscier D.G., Mould S.J., Doehner H., RA Doehner K., Rommens J.M., Vincent J.B., Venter J.C., Li P.W., Mural R.J., RA Adams M.D., Tsui L.-C.; RT "Human chromosome 7: DNA sequence and biology."; RL Science 300:767-772(2003). RN [7] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M., RA Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J., RA Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S., RA Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H., RA Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K., RA Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D., RA Hunkapiller M.W., Myers E.W., Venter J.C.; RL Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases. RN [8] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1). RC TISSUE=Pancreas; RX PubMed=15489334; DOI=10.1101/gr.2596504; RG The MGC Project Team; RT "The status, quality, and expansion of the NIH full-length cDNA project: RT the Mammalian Gene Collection (MGC)."; RL Genome Res. 14:2121-2127(2004). RN [9] RP IDENTIFICATION (ISOFORM 4), FUNCTION (ISOFORM 4), IDENTIFICATION IN A RP TFIID-LIKE COMPLEX (ISOFORM 4), INDUCTION (ISOFORM 4), AND CLEAVAGE RP (ISOFORM 4). RX PubMed=11583621; DOI=10.1016/s1097-2765(01)00325-2; RA Bell B., Scheer E., Tora L.; RT "Identification of hTAF(II)80 delta links apoptotic signaling pathways to RT transcription factor TFIID function."; RL Mol. Cell 8:591-600(2001). RN [10] RP IDENTIFICATION IN THE TFTC-HAT COMPLEX, AND IDENTIFICATION BY MASS RP SPECTROMETRY. RX PubMed=12601814; DOI=10.1002/pmic.200390030; RA Cavusoglu N., Brand M., Tora L., van Dorsselaer A.; RT "Novel subunits of the TATA binding protein free TAFII-containing RT transcription complex identified by matrix-assisted laser RT desorption/ionization-time of flight mass spectrometry following one- RT dimensional gel electrophoresis."; RL Proteomics 3:217-223(2003). RN [11] RP IDENTIFICATION IN THE MLL1/MLL COMPLEX. RX PubMed=15960975; DOI=10.1016/j.cell.2005.04.031; RA Dou Y., Milne T.A., Tackett A.J., Smith E.R., Fukuda A., Wysocka J., RA Allis C.D., Chait B.T., Hess J.L., Roeder R.G.; RT "Physical association and coordinate function of the H3 K4 RT methyltransferase MLL1 and the H4 K16 acetyltransferase MOF."; RL Cell 121:873-885(2005). RN [12] RP INTERACTION WITH TAF9 IN A COMPLEX WITH TAF6; TAF9; TAF12 AND TAF4B, AND RP DNA-BINDING. RX PubMed=15601843; DOI=10.1128/mcb.25.1.206-219.2005; RA Shao H., Revach M., Moshonov S., Tzuman Y., Gazit K., Albeck S., Unger T., RA Dikstein R.; RT "Core promoter binding by histone-like TAF complexes."; RL Mol. Cell. Biol. 25:206-219(2005). RN [13] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-653 AND THR-660, AND RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Cervix carcinoma; RX PubMed=16964243; DOI=10.1038/nbt1240; RA Beausoleil S.A., Villen J., Gerber S.A., Rush J., Gygi S.P.; RT "A probability-based approach for high-throughput protein phosphorylation RT analysis and site localization."; RL Nat. Biotechnol. 24:1285-1292(2006). RN [14] RP FUNCTION (ISOFORM 4), AND SUBCELLULAR LOCATION (ISOFORM 4). RX PubMed=18628956; DOI=10.1371/journal.pone.0002721; RA Wilhelm E., Pellay F.X., Benecke A., Bell B.; RT "TAF6delta controls apoptosis and gene expression in the absence of p53."; RL PLoS ONE 3:E2721-E2721(2008). RN [15] RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Cervix carcinoma; RX PubMed=18669648; DOI=10.1073/pnas.0805139105; RA Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E., RA Elledge S.J., Gygi S.P.; RT "A quantitative atlas of mitotic phosphorylation."; RL Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008). RN [16] RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RX PubMed=19413330; DOI=10.1021/ac9004309; RA Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S.; RT "Lys-N and trypsin cover complementary parts of the phosphoproteome in a RT refined SCX-based approach."; RL Anal. Chem. 81:4493-4501(2009). RN [17] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-653 AND THR-660, AND RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Leukemic T-cell; RX PubMed=19690332; DOI=10.1126/scisignal.2000007; RA Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K., RA Rodionov V., Han D.K.; RT "Quantitative phosphoproteomic analysis of T cell receptor signaling RT reveals system-wide modulation of protein-protein interactions."; RL Sci. Signal. 2:RA46-RA46(2009). RN [18] RP FUNCTION (ISOFORM 4), AND INTERACTION WITH TP53 (ISOFORMS 1 AND 4). RX PubMed=20096117; DOI=10.1186/1471-2199-11-10; RA Wilhelm E., Kornete M., Targat B., Vigneault-Edwards J., Frontini M., RA Tora L., Benecke A., Bell B.; RT "TAF6delta orchestrates an apoptotic transcriptome profile and interacts RT functionally with p53."; RL BMC Mol. Biol. 11:10-10(2010). RN [19] RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Cervix carcinoma; RX PubMed=20068231; DOI=10.1126/scisignal.2000475; RA Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L., RA Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M.; RT "Quantitative phosphoproteomics reveals widespread full phosphorylation RT site occupancy during mitosis."; RL Sci. Signal. 3:RA3-RA3(2010). RN [20] RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RX PubMed=21269460; DOI=10.1186/1752-0509-5-17; RA Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T., RA Bennett K.L., Superti-Furga G., Colinge J.; RT "Initial characterization of the human central proteome."; RL BMC Syst. Biol. 5:17-17(2011). RN [21] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-120; SER-634; SER-636; RP SER-653 AND THR-660, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE RP ANALYSIS]. RC TISSUE=Cervix carcinoma, and Erythroleukemia; RX PubMed=23186163; DOI=10.1021/pr300630k; RA Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J., RA Mohammed S.; RT "Toward a comprehensive characterization of a human cancer cell RT phosphoproteome."; RL J. Proteome Res. 12:260-271(2013). RN [22] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-653 AND THR-660, AND RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Liver; RX PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014; RA Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L., RA Ye M., Zou H.; RT "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver RT phosphoproteome."; RL J. Proteomics 96:253-262(2014). RN [23] RP METHYLATION [LARGE SCALE ANALYSIS] AT ARG-524, AND IDENTIFICATION BY MASS RP SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Colon carcinoma; RX PubMed=24129315; DOI=10.1074/mcp.o113.027870; RA Guo A., Gu H., Zhou J., Mulhern D., Wang Y., Lee K.A., Yang V., Aguiar M., RA Kornhauser J., Jia X., Ren J., Beausoleil S.A., Silva J.C., Vemulapalli V., RA Bedford M.T., Comb M.J.; RT "Immunoaffinity enrichment and mass spectrometry analysis of protein RT methylation."; RL Mol. Cell. Proteomics 13:372-387(2014). RN [24] RP ALTERNATIVE SPLICING (ISOFORM 4). RX PubMed=25025302; DOI=10.1371/journal.pone.0102399; RA Kamtchueng C., Stebenne M.E., Delannoy A., Wilhelm E., Leger H., RA Benecke A.G., Bell B.; RT "Alternative splicing of TAF6: downstream transcriptome impacts and RT upstream RNA splice control elements."; RL PLoS ONE 9:E102399-E102399(2014). RN [25] RP FUNCTION (ISOFORM 4). RX PubMed=29358700; DOI=10.1038/s41419-017-0115-3; RA Delannoy A., Wilhelm E., Eilebrecht S., Alvarado-Cuevas E.M., Benecke A.G., RA Bell B.; RT "BIM and NOXA are mitochondrial effectors of TAF6delta-driven apoptosis."; RL Cell Death Dis. 9:70-70(2018). RN [26] RP INVOLVEMENT IN ALYUS, AND VARIANT ALYUS THR-71. RX PubMed=25558065; DOI=10.1016/j.celrep.2014.12.015; RA Alazami A.M., Patel N., Shamseldin H.E., Anazi S., Al-Dosari M.S., RA Alzahrani F., Hijazi H., Alshammari M., Aldahmesh M.A., Salih M.A., RA Faqeih E., Alhashem A., Bashiri F.A., Al-Owain M., Kentab A.Y., Sogaty S., RA Al Tala S., Temsah M.H., Tulbah M., Aljelaify R.F., Alshahwan S.A., RA Seidahmed M.Z., Alhadid A.A., Aldhalaan H., Alqallaf F., Kurdi W., RA Alfadhel M., Babay Z., Alsogheer M., Kaya N., Al-Hassnan Z.N., RA Abdel-Salam G.M., Al-Sannaa N., Al Mutairi F., El Khashab H.Y., Bohlega S., RA Jia X., Nguyen H.C., Hammami R., Adly N., Mohamed J.Y., Abdulwahab F., RA Ibrahim N., Naim E.A., Al-Younes B., Meyer B.F., Hashem M., Shaheen R., RA Xiong Y., Abouelhoda M., Aldeeri A.A., Monies D.M., Alkuraya F.S.; RT "Accelerating novel candidate gene discovery in neurogenetic disorders via RT whole-exome sequencing of prescreened multiplex consanguineous families."; RL Cell Rep. 10:148-161(2015). RN [27] RP INVOLVEMENT IN ALYUS, VARIANTS ALYUS CYS-46 AND THR-71, AND RP CHARACTERIZATION OF VARIANTS ALYUS CYS-46 AND THR-71. RX PubMed=25574841; DOI=10.1172/jci77435; RA Yuan B., Pehlivan D., Karaca E., Patel N., Charng W.L., Gambin T., RA Gonzaga-Jauregui C., Sutton V.R., Yesil G., Bozdogan S.T., Tos T., RA Koparir A., Koparir E., Beck C.R., Gu S., Aslan H., Yuregir O.O., RA Al Rubeaan K., Alnaqeb D., Alshammari M.J., Bayram Y., Atik M.M., Aydin H., RA Geckinli B.B., Seven M., Ulucan H., Fenercioglu E., Ozen M., Jhangiani S., RA Muzny D.M., Boerwinkle E., Tuysuz B., Alkuraya F.S., Gibbs R.A., RA Lupski J.R.; RT "Global transcriptional disturbances underlie Cornelia de Lange syndrome RT and related phenotypes."; RL J. Clin. Invest. 125:636-651(2015). RN [28] RP SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-196, AND IDENTIFICATION BY MASS RP SPECTROMETRY [LARGE SCALE ANALYSIS]. RX PubMed=28112733; DOI=10.1038/nsmb.3366; RA Hendriks I.A., Lyon D., Young C., Jensen L.J., Vertegaal A.C., RA Nielsen M.L.; RT "Site-specific mapping of the human SUMO proteome reveals co-modification RT with phosphorylation."; RL Nat. Struct. Mol. Biol. 24:325-336(2017). RN [29] {ECO:0007744|PDB:7EDX, ECO:0007744|PDB:7EG7, ECO:0007744|PDB:7EG8, ECO:0007744|PDB:7EG9, ECO:0007744|PDB:7EGA, ECO:0007744|PDB:7EGB, ECO:0007744|PDB:7EGC, ECO:0007744|PDB:7EGD, ECO:0007744|PDB:7EGE, ECO:0007744|PDB:7EGF} RP STRUCTURE BY ELECTRON MICROSCOPY (2.77 ANGSTROMS), FUNCTION, IDENTIFICATION RP IN THE TFIID COMPLEX, AND SUBUNIT. RX PubMed=33795473; DOI=10.1126/science.aba8490; RA Chen X., Qi Y., Wu Z., Wang X., Li J., Zhao D., Hou H., Li Y., Yu Z., RA Liu W., Wang M., Ren Y., Li Z., Yang H., Xu Y.; RT "Structural insights into preinitiation complex assembly on core RT promoters."; RL Science 372:0-0(2021). CC -!- FUNCTION: The TFIID basal transcription factor complex plays a major CC role in the initiation of RNA polymerase II (Pol II)-dependent CC transcription (PubMed:33795473). TFIID recognizes and binds promoters CC with or without a TATA box via its subunit TBP, a TATA-box-binding CC protein, and promotes assembly of the pre-initiation complex (PIC) CC (PubMed:33795473). The TFIID complex consists of TBP and TBP-associated CC factors (TAFs), including TAF1, TAF2, TAF3, TAF4, TAF5, TAF6, TAF7, CC TAF8, TAF9, TAF10, TAF11, TAF12 and TAF13 (PubMed:33795473). The TFIID CC complex structure can be divided into 3 modules TFIID-A, TFIID-B, and CC TFIID-C (PubMed:33795473). TAF6 homodimer connects TFIID modules, CC forming a rigid core (PubMed:33795473). {ECO:0000269|PubMed:33795473}. CC -!- FUNCTION: [Isoform 4]: Transcriptional regulator which acts primarily CC as a positive regulator of transcription (PubMed:20096117, CC PubMed:29358700). Recruited to the promoters of a number of genes CC including GADD45A and CDKN1A/p21, leading to transcriptional up- CC regulation and subsequent induction of apoptosis (PubMed:11583621). CC Also up-regulates expression of other genes including GCNA/ACRC, HES1 CC and IFFO1 (PubMed:18628956). In contrast, down-regulates transcription CC of MDM2 (PubMed:11583621). Acts as a transcriptional coactivator to CC enhance transcription of TP53/p53-responsive genes such as DUSP1 CC (PubMed:20096117). Can also activate transcription and apoptosis CC independently of TP53 (PubMed:18628956). Drives apoptosis via the CC intrinsic apoptotic pathway by up-regulating apoptosis effectors such CC as BCL2L11/BIM and PMAIP1/NOXA (PubMed:29358700). CC {ECO:0000269|PubMed:11583621, ECO:0000269|PubMed:18628956, CC ECO:0000269|PubMed:20096117, ECO:0000269|PubMed:29358700}. CC -!- SUBUNIT: Component of the TFIID basal transcription factor complex, CC composed of TATA-box-binding protein TBP, and a number of TBP- CC associated factors (TAFs), including TAF1, TAF2, TAF3, TAF4, TAF5, CC TAF6, TAF7, TAF8, TAF9, TAF10, TAF11, TAF12 and TAF13 (PubMed:33795473, CC PubMed:8262073). Interacts directly with TBP, TAF1/TAFII250, CC TAF9/TAFII31 and TAF12/TAFII20 (PubMed:7667268). The TAF6/TAFII70- CC TAF9/TAFII31 heterodimer forms an octamer complex with the CC TAF4B/TFII105-TAF12/TFIID20 heterodimer (PubMed:15601843). Component of CC some MLL1/MLL complex, at least composed of the core components CC KMT2A/MLL1, ASH2L, HCFC1/HCF1, WDR5 and RBBP5, as well as the CC facultative components BACC1, CHD8, E2F6, HSP70, INO80C, KANSL1, LAS1L, CC MAX, MCRS1, MGA, MYST1/MOF, PELP1, PHF20, PRP31, RING2, RUVB1/TIP49A, CC RUVB2/TIP49B, SENP3, TAF1, TAF4, TAF6, TAF7, TAF9 and TEX10 CC (PubMed:15960975). Also interacts with the GTFs, TFIIEalpha/GTF2E1 and CC TFIIFalpha/GTF2F1 (PubMed:7667268). Component of the TBP-free TAFII- CC histone acetylase complex (TFTC-HAT) (PubMed:12601814). CC {ECO:0000269|PubMed:12601814, ECO:0000269|PubMed:15601843, CC ECO:0000269|PubMed:15960975, ECO:0000269|PubMed:33795473, CC ECO:0000269|PubMed:7667268, ECO:0000269|PubMed:8262073}. CC -!- SUBUNIT: [Isoform 1]: Interacts with TP53/p53. CC {ECO:0000269|PubMed:20096117}. CC -!- SUBUNIT: [Isoform 4]: Not part of the TBP-free TAFII-histone acetylase CC complex (TFTC-HAT) (PubMed:11583621). Part of a TFIID-like complex CC which lacks TAF9 (PubMed:11583621). Interacts with TP53/p53 CC (PubMed:20096117). {ECO:0000269|PubMed:11583621, CC ECO:0000269|PubMed:20096117}. CC -!- INTERACTION: CC P49848; Q1K9H5: PB1; Xeno; NbExp=2; IntAct=EBI-1560206, EBI-6050669; CC P49848-3; Q8N9N5-2: BANP; NbExp=3; IntAct=EBI-12940148, EBI-11524452; CC P49848-3; Q8WWB5: PIH1D2; NbExp=3; IntAct=EBI-12940148, EBI-10232538; CC -!- SUBCELLULAR LOCATION: Nucleus. CC -!- SUBCELLULAR LOCATION: [Isoform 4]: Nucleus CC {ECO:0000269|PubMed:18628956}. CC -!- ALTERNATIVE PRODUCTS: CC Event=Alternative splicing; Named isoforms=4; CC Name=1; Synonyms=Alpha {ECO:0000303|PubMed:8262073}; CC IsoId=P49848-1; Sequence=Displayed; CC Name=2; Synonyms=Gamma {ECO:0000303|PubMed:8262073}; CC IsoId=P49848-2; Sequence=VSP_037476; CC Name=3; CC IsoId=P49848-3; Sequence=VSP_043709; CC Name=4; Synonyms=Delta {ECO:0000303|PubMed:11583621, CC ECO:0000303|PubMed:25025302}; CC IsoId=P49848-4; Sequence=VSP_059851; CC -!- INDUCTION: [Isoform 4]: Induced in cells undergoing apoptosis. CC {ECO:0000269|PubMed:11583621}. CC -!- PTM: [Isoform 4]: In cells undergoing apoptosis, cleaved in a caspase- CC dependent manner to produce a 40 kDa product. CC {ECO:0000269|PubMed:11583621}. CC -!- DISEASE: Alazami-Yuan syndrome (ALYUS) [MIM:617126]: An autosomal CC recessive syndrome reminiscent of Cornelia de Lange syndrome and CC characterized by delayed psychomotor development with intellectual CC disability, hypotonia, microcephaly, short stature, poor speech, and CC dysmorphic features. {ECO:0000269|PubMed:25558065, CC ECO:0000269|PubMed:25574841}. Note=The disease is caused by variants CC affecting the gene represented in this entry. CC -!- SIMILARITY: Belongs to the TAF6 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; L25444; AAA63643.1; -; mRNA. DR EMBL; U31659; AAA84390.1; -; mRNA. DR EMBL; AK300005; BAG61823.1; -; mRNA. DR EMBL; CR627390; CAH10485.1; -; mRNA. DR EMBL; AY149894; AAN10295.1; -; Genomic_DNA. DR EMBL; CH236956; EAL23851.1; -; Genomic_DNA. DR EMBL; CH236956; EAL23852.1; -; Genomic_DNA. DR EMBL; CH471091; EAW76589.1; -; Genomic_DNA. DR EMBL; CH471091; EAW76591.1; -; Genomic_DNA. DR EMBL; CH471091; EAW76592.1; -; Genomic_DNA. DR EMBL; BC018115; AAH18115.1; -; mRNA. DR CCDS; CCDS55135.1; -. [P49848-3] DR CCDS; CCDS5686.1; -. [P49848-1] DR CCDS; CCDS94153.1; -. [P49848-4] DR RefSeq; NP_001177344.1; NM_001190415.2. [P49848-3] DR RefSeq; NP_001351927.1; NM_001364998.1. [P49848-1] DR RefSeq; NP_001351928.1; NM_001364999.1. [P49848-1] DR RefSeq; NP_001351929.1; NM_001365000.1. [P49848-4] DR RefSeq; NP_001351930.1; NM_001365001.1. [P49848-4] DR RefSeq; NP_001351931.1; NM_001365002.1. [P49848-4] DR RefSeq; NP_001351932.1; NM_001365003.1. [P49848-4] DR RefSeq; NP_005632.1; NM_005641.4. [P49848-1] DR RefSeq; NP_647476.1; NM_139315.3. [P49848-1] DR RefSeq; XP_011514845.1; XM_011516543.4. [P49848-4] DR RefSeq; XP_024302664.1; XM_024446896.2. [P49848-1] DR RefSeq; XP_024302668.1; XM_024446900.2. [P49848-1] DR RefSeq; XP_047276735.1; XM_047420779.1. [P49848-1] DR RefSeq; XP_047276736.1; XM_047420780.1. [P49848-4] DR RefSeq; XP_047276737.1; XM_047420781.1. [P49848-4] DR RefSeq; XP_054214873.1; XM_054358898.1. [P49848-1] DR RefSeq; XP_054214874.1; XM_054358899.1. [P49848-4] DR RefSeq; XP_054214875.1; XM_054358900.1. [P49848-1] DR RefSeq; XP_054214876.1; XM_054358901.1. [P49848-4] DR RefSeq; XP_054214878.1; XM_054358903.1. [P49848-1] DR RefSeq; XP_054214879.1; XM_054358904.1. [P49848-4] DR PDB; 5FUR; EM; 8.50 A; J/K=1-677. DR PDB; 6F3T; X-ray; 2.50 A; E/G/I/K=5-92. DR PDB; 6MZC; EM; 4.50 A; H/I=1-677. DR PDB; 6MZD; EM; 9.80 A; H=1-677. DR PDB; 6MZL; EM; 23.00 A; H/I=1-677. DR PDB; 6MZM; EM; 7.50 A; H/I=1-677. DR PDB; 7EDX; EM; 4.50 A; F/f=1-677. DR PDB; 7EG7; EM; 6.20 A; F/f=1-677. DR PDB; 7EG8; EM; 7.40 A; F/f=1-677. DR PDB; 7EG9; EM; 3.70 A; F/f=1-677. DR PDB; 7EGA; EM; 4.10 A; F/f=1-677. DR PDB; 7EGB; EM; 3.30 A; F/f=1-677. DR PDB; 7EGC; EM; 3.90 A; F/f=1-677. DR PDB; 7EGD; EM; 6.75 A; F/f=1-677. DR PDB; 7EGE; EM; 9.00 A; F/f=1-677. DR PDB; 7EGF; EM; 3.16 A; f=1-677. DR PDB; 7EGG; EM; 2.77 A; F=1-677. DR PDB; 7EGH; EM; 3.04 A; F/f=1-677. DR PDB; 7EGI; EM; 9.82 A; F/f=1-677. DR PDB; 7EGJ; EM; 8.64 A; F/f=1-677. DR PDB; 7ENA; EM; 4.07 A; DF/Df=1-677. DR PDB; 7ENC; EM; 4.13 A; DF/Df=1-677. DR PDB; 8GXQ; EM; 5.04 A; DF/Df=1-677. DR PDB; 8GXS; EM; 4.16 A; DF/Df=1-677. DR PDB; 8WAK; EM; 5.47 A; F/f=1-677. DR PDB; 8WAL; EM; 8.52 A; F/f=1-677. DR PDB; 8WAN; EM; 6.07 A; F/f=1-677. DR PDB; 8WAO; EM; 6.40 A; F/f=1-677. DR PDB; 8WAP; EM; 5.85 A; F/f=1-677. DR PDB; 8WAQ; EM; 6.29 A; F/f=1-677. DR PDB; 8WAR; EM; 7.20 A; F/f=1-677. DR PDB; 8WAS; EM; 6.13 A; F/f=1-677. DR AlphaFoldDB; P49848; -. DR EMDB; EMD-31075; -. DR EMDB; EMD-31107; -. DR EMDB; EMD-31108; -. DR EMDB; EMD-31109; -. DR EMDB; EMD-31110; -. DR EMDB; EMD-31111; -. DR EMDB; EMD-31112; -. DR EMDB; EMD-31113; -. DR EMDB; EMD-31114; -. DR EMDB; EMD-31115; -. DR EMDB; EMD-31116; -. DR EMDB; EMD-31117; -. DR EMDB; EMD-31118; -. DR EMDB; EMD-31119; -. DR EMDB; EMD-31204; -. DR EMDB; EMD-31207; -. DR EMDB; EMD-34359; -. DR EMDB; EMD-34360; -. DR EMDB; EMD-37395; -. DR EMDB; EMD-37396; -. DR EMDB; EMD-37398; -. DR EMDB; EMD-37399; -. DR EMDB; EMD-37400; -. DR EMDB; EMD-37401; -. DR EMDB; EMD-37402; -. DR EMDB; EMD-37403; -. DR EMDB; EMD-9298; -. DR EMDB; EMD-9302; -. DR EMDB; EMD-9305; -. DR EMDB; EMD-9306; -. DR SMR; P49848; -. DR BioGRID; 112741; 247. DR ComplexPortal; CPX-903; TFTC histone acetylation complex. DR ComplexPortal; CPX-915; General transcription factor complex TFIID. DR ComplexPortal; CPX-930; General transcription factor complex TFIID, TAF4B variant. DR CORUM; P49848; -. DR DIP; DIP-773N; -. DR FunCoup; P49848; 2593. DR IntAct; P49848; 78. DR MINT; P49848; -. DR NDEx; IQUERY-CP-TAF6; 2 NDEx IQuery Curated Pathways. DR STRING; 9606.ENSP00000399982; -. DR ChEMBL; CHEMBL5465548; -. DR GlyCosmos; P49848; 15 sites, 2 glycans. DR GlyGen; P49848; 19 sites, 2 O-linked glycans (19 sites). DR iPTMnet; P49848; -. DR MetOSite; P49848; -. DR PhosphoSitePlus; P49848; -. DR BioMuta; TAF6; -. DR DMDM; 1729810; -. DR jPOST; P49848; -. DR MassIVE; P49848; -. DR PaxDb; 9606-ENSP00000399982; -. DR PeptideAtlas; P49848; -. DR ProteomicsDB; 56157; -. [P49848-1] DR ProteomicsDB; 56158; -. [P49848-2] DR ProteomicsDB; 56159; -. [P49848-3] DR Pumba; P49848; -. DR Antibodypedia; 1765; 202 antibodies from 24 providers. DR DNASU; 6878; -. DR Ensembl; ENST00000344095.8; ENSP00000344537.4; ENSG00000106290.17. [P49848-1] DR Ensembl; ENST00000437822.6; ENSP00000399982.2; ENSG00000106290.17. [P49848-3] DR Ensembl; ENST00000452041.5; ENSP00000416396.1; ENSG00000106290.17. [P49848-1] DR Ensembl; ENST00000453269.7; ENSP00000389575.2; ENSG00000106290.17. [P49848-1] DR Ensembl; ENST00000460673.3; ENSP00000427710.3; ENSG00000106290.17. [P49848-1] DR Ensembl; ENST00000472509.6; ENSP00000419760.2; ENSG00000106290.17. [P49848-1] DR Ensembl; ENST00000685280.1; ENSP00000510209.1; ENSG00000106290.17. [P49848-1] DR Ensembl; ENST00000686172.1; ENSP00000510809.1; ENSG00000106290.17. [P49848-4] DR Ensembl; ENST00000686580.1; ENSP00000510270.1; ENSG00000106290.17. [P49848-1] DR Ensembl; ENST00000686777.1; ENSP00000510166.1; ENSG00000106290.17. [P49848-1] DR Ensembl; ENST00000687137.1; ENSP00000508432.1; ENSG00000106290.17. [P49848-1] DR Ensembl; ENST00000687151.1; ENSP00000508852.1; ENSG00000106290.17. [P49848-4] DR Ensembl; ENST00000687410.1; ENSP00000509158.1; ENSG00000106290.17. [P49848-1] DR Ensembl; ENST00000687447.1; ENSP00000510217.1; ENSG00000106290.17. [P49848-1] DR Ensembl; ENST00000687672.1; ENSP00000509741.1; ENSG00000106290.17. [P49848-4] DR Ensembl; ENST00000687969.1; ENSP00000508679.1; ENSG00000106290.17. [P49848-1] DR Ensembl; ENST00000688343.1; ENSP00000508691.1; ENSG00000106290.17. [P49848-1] DR Ensembl; ENST00000688498.1; ENSP00000510409.1; ENSG00000106290.17. [P49848-1] DR Ensembl; ENST00000688640.1; ENSP00000509783.1; ENSG00000106290.17. [P49848-1] DR Ensembl; ENST00000689754.1; ENSP00000509866.1; ENSG00000106290.17. [P49848-1] DR Ensembl; ENST00000690367.1; ENSP00000509821.1; ENSG00000106290.17. [P49848-4] DR Ensembl; ENST00000691010.1; ENSP00000509320.1; ENSG00000106290.17. [P49848-4] DR Ensembl; ENST00000691370.1; ENSP00000509500.1; ENSG00000106290.17. [P49848-1] DR Ensembl; ENST00000691681.1; ENSP00000509494.1; ENSG00000106290.17. [P49848-1] DR Ensembl; ENST00000692408.1; ENSP00000508788.1; ENSG00000106290.17. [P49848-4] DR Ensembl; ENST00000692466.1; ENSP00000509041.1; ENSG00000106290.17. [P49848-1] DR Ensembl; ENST00000692927.1; ENSP00000509335.1; ENSG00000106290.17. [P49848-1] DR Ensembl; ENST00000907010.1; ENSP00000577069.1; ENSG00000106290.17. [P49848-1] DR Ensembl; ENST00000907012.1; ENSP00000577071.1; ENSG00000106290.17. [P49848-4] DR Ensembl; ENST00000907013.1; ENSP00000577072.1; ENSG00000106290.17. [P49848-1] DR Ensembl; ENST00000907016.1; ENSP00000577075.1; ENSG00000106290.17. [P49848-1] DR Ensembl; ENST00000907019.1; ENSP00000577078.1; ENSG00000106290.17. [P49848-4] DR Ensembl; ENST00000907020.1; ENSP00000577079.1; ENSG00000106290.17. [P49848-1] DR Ensembl; ENST00000907021.1; ENSP00000577080.1; ENSG00000106290.17. [P49848-4] DR Ensembl; ENST00000907022.1; ENSP00000577081.1; ENSG00000106290.17. [P49848-1] DR Ensembl; ENST00000907023.1; ENSP00000577082.1; ENSG00000106290.17. [P49848-4] DR Ensembl; ENST00000907025.1; ENSP00000577084.1; ENSG00000106290.17. [P49848-4] DR Ensembl; ENST00000907027.1; ENSP00000577086.1; ENSG00000106290.17. [P49848-1] DR Ensembl; ENST00000907028.1; ENSP00000577087.1; ENSG00000106290.17. [P49848-1] DR Ensembl; ENST00000918699.1; ENSP00000588758.1; ENSG00000106290.17. [P49848-4] DR Ensembl; ENST00000918702.1; ENSP00000588761.1; ENSG00000106290.17. [P49848-4] DR Ensembl; ENST00000918703.1; ENSP00000588762.1; ENSG00000106290.17. [P49848-1] DR Ensembl; ENST00000918706.1; ENSP00000588765.1; ENSG00000106290.17. [P49848-4] DR Ensembl; ENST00000918708.1; ENSP00000588767.1; ENSG00000106290.17. [P49848-4] DR Ensembl; ENST00000918709.1; ENSP00000588768.1; ENSG00000106290.17. [P49848-2] DR Ensembl; ENST00000918710.1; ENSP00000588769.1; ENSG00000106290.17. [P49848-4] DR Ensembl; ENST00000918714.1; ENSP00000588773.1; ENSG00000106290.17. [P49848-1] DR Ensembl; ENST00000918715.1; ENSP00000588774.1; ENSG00000106290.17. [P49848-4] DR Ensembl; ENST00000918721.1; ENSP00000588780.1; ENSG00000106290.17. [P49848-4] DR Ensembl; ENST00000918722.1; ENSP00000588781.1; ENSG00000106290.17. [P49848-1] DR Ensembl; ENST00000918723.1; ENSP00000588782.1; ENSG00000106290.17. [P49848-1] DR GeneID; 6878; -. DR KEGG; hsa:6878; -. DR MANE-Select; ENST00000453269.7; ENSP00000389575.2; NM_139315.3; NP_647476.1. DR UCSC; uc003uti.4; human. [P49848-1] DR AGR; HGNC:11540; -. DR ClinPGx; PA36315; -. DR CTD; 6878; -. DR DisGeNET; 6878; -. DR GeneCards; TAF6; -. DR HGNC; HGNC:11540; TAF6. DR HPA; ENSG00000106290; Low tissue specificity. DR MalaCards; TAF6; -. DR MIM; 602955; gene. DR MIM; 617126; phenotype. DR OpenTargets; ENSG00000106290; -. DR Orphanet; 694946; Alazami-Yuan syndrome. DR VEuPathDB; HostDB:ENSG00000106290; -. DR eggNOG; KOG2549; Eukaryota. DR GeneTree; ENSGT00640000091486; -. DR HOGENOM; CLU_021711_2_1_1; -. DR InParanoid; P49848; -. DR OMA; MPEETCQ; -. DR OrthoDB; 361039at2759; -. DR PAN-GO; P49848; 4 GO annotations based on evolutionary models. DR PhylomeDB; P49848; -. DR PathwayCommons; P49848; -. DR Reactome; R-HSA-167161; HIV Transcription Initiation. DR Reactome; R-HSA-167162; RNA Polymerase II HIV Promoter Escape. DR Reactome; R-HSA-167172; Transcription of the HIV genome. DR Reactome; R-HSA-674695; RNA Polymerase II Pre-transcription Events. DR Reactome; R-HSA-6804756; Regulation of TP53 Activity through Phosphorylation. DR Reactome; R-HSA-6807505; RNA polymerase II transcribes snRNA genes. DR Reactome; R-HSA-73776; RNA Polymerase II Promoter Escape. DR Reactome; R-HSA-73779; RNA Polymerase II Transcription Pre-Initiation And Promoter Opening. DR Reactome; R-HSA-75953; RNA Polymerase II Transcription Initiation. DR Reactome; R-HSA-76042; RNA Polymerase II Transcription Initiation And Promoter Clearance. DR SignaLink; P49848; -. DR SIGNOR; P49848; -. DR Agora; ENSG00000106290; -. DR BioGRID-ORCS; 6878; 733 hits in 1143 CRISPR screens. DR ChiTaRS; TAF6; human. DR GeneWiki; TAF6; -. DR GenomeRNAi; 6878; -. DR Pharos; P49848; Tbio. DR PRO; PR:P49848; -. DR Proteomes; UP000005640; Chromosome 7. DR RNAct; P49848; protein. DR Bgee; ENSG00000106290; Expressed in stromal cell of endometrium and 206 other cell types or tissues. DR ExpressionAtlas; P49848; baseline and differential. DR GO; GO:0071339; C:MLL1 complex; IDA:UniProtKB. DR GO; GO:0005654; C:nucleoplasm; IDA:HPA. DR GO; GO:0005634; C:nucleus; IDA:UniProtKB. DR GO; GO:0032991; C:protein-containing complex; IMP:CAFA. DR GO; GO:0000124; C:SAGA complex; IEA:InterPro. DR GO; GO:0046695; C:SLIK (SAGA-like) complex; IEA:InterPro. DR GO; GO:0005669; C:transcription factor TFIID complex; IDA:UniProtKB. DR GO; GO:0033276; C:transcription factor TFTC complex; IDA:UniProtKB. DR GO; GO:0017162; F:aryl hydrocarbon receptor binding; IPI:CAFA. DR GO; GO:0003677; F:DNA binding; IDA:UniProtKB. DR GO; GO:0046982; F:protein heterodimerization activity; IEA:InterPro. DR GO; GO:0016251; F:RNA polymerase II general transcription initiation factor activity; IDA:GO_Central. DR GO; GO:0003713; F:transcription coactivator activity; IBA:GO_Central. DR GO; GO:0006352; P:DNA-templated transcription initiation; IDA:UniProtKB. DR GO; GO:0042789; P:mRNA transcription by RNA polymerase II; IDA:ComplexPortal. DR GO; GO:0045786; P:negative regulation of cell cycle; IDA:UniProtKB. DR GO; GO:0008285; P:negative regulation of cell population proliferation; IDA:UniProtKB. DR GO; GO:0043065; P:positive regulation of apoptotic process; IDA:UniProtKB. DR GO; GO:0045893; P:positive regulation of DNA-templated transcription; NAS:ComplexPortal. DR GO; GO:2001244; P:positive regulation of intrinsic apoptotic signaling pathway; IDA:UniProtKB. DR GO; GO:0060261; P:positive regulation of transcription initiation by RNA polymerase II; IDA:UniProtKB. DR GO; GO:0006282; P:regulation of DNA repair; NAS: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; NAS:UniProtKB. DR GO; GO:0006367; P:transcription initiation at RNA polymerase II promoter; IDA:UniProtKB. DR CDD; cd22931; HFD_TAF6; 1. DR CDD; cd08050; TAF6C; 1. DR DisProt; DP01262; -. DR FunFam; 1.10.20.10:FF:000030; Transcription initiation factor TFIID subunit 6; 1. DR FunFam; 1.25.40.770:FF:000001; Transcription initiation factor TFIID subunit 6; 1. DR Gene3D; 1.10.20.10; Histone, subunit A; 1. DR Gene3D; 1.25.40.770; TAF6, C-terminal HEAT repeat domain; 1. DR InterPro; IPR016024; ARM-type_fold. DR InterPro; IPR009072; Histone-fold. DR InterPro; IPR037796; TAF6. DR InterPro; IPR011442; TAF6_C. DR InterPro; IPR046344; TAF6_C_sf. DR InterPro; IPR004823; TAF_TATA-bd_Histone-like_dom. DR PANTHER; PTHR10221; TRANSCRIPTION INITIATION FACTOR TFIID SUBUNIT 6; 1. DR PANTHER; PTHR10221:SF9; TRANSCRIPTION INITIATION FACTOR TFIID SUBUNIT 6; 1. DR Pfam; PF02969; TAF; 1. DR Pfam; PF07571; TAF6_C; 1. DR SMART; SM00803; TAF; 1. DR SUPFAM; SSF48371; ARM repeat; 1. DR SUPFAM; SSF47113; Histone-fold; 1. DR PDBsum; 5FUR; -. DR PDBsum; 6F3T; -. DR PDBsum; 6MZC; -. DR PDBsum; 6MZD; -. DR PDBsum; 6MZL; -. DR PDBsum; 6MZM; -. DR PDBsum; 7EDX; -. DR PDBsum; 7EG7; -. DR PDBsum; 7EG8; -. DR PDBsum; 7EG9; -. DR PDBsum; 7EGA; -. DR PDBsum; 7EGB; -. DR PDBsum; 7EGC; -. DR PDBsum; 7EGD; -. DR PDBsum; 7EGE; -. DR PDBsum; 7EGF; -. DR PDBsum; 7EGG; -. DR PDBsum; 7EGH; -. DR PDBsum; 7EGI; -. DR PDBsum; 7EGJ; -. DR PDBsum; 7ENA; -. DR PDBsum; 7ENC; -. DR PDBsum; 8GXQ; -. DR PDBsum; 8GXS; -. DR PDBsum; 8WAK; -. DR PDBsum; 8WAL; -. DR PDBsum; 8WAN; -. DR PDBsum; 8WAO; -. DR PDBsum; 8WAP; -. DR PDBsum; 8WAQ; -. DR PDBsum; 8WAR; -. DR PDBsum; 8WAS; -. PE 1: Evidence at protein level; KW 3D-structure; Alternative splicing; Apoptosis; Direct protein sequencing; KW Disease variant; Intellectual disability; Isopeptide bond; Methylation; KW Nucleus; Phosphoprotein; Proteomics identification; Reference proteome; KW Transcription; Transcription regulation; Ubl conjugation. FT CHAIN 1..677 FT /note="Transcription initiation factor TFIID subunit 6" FT /id="PRO_0000118873" FT REGION 142..204 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 524..574 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 611..677 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 554..574 FT /note="Low complexity" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 624..634 FT /note="Pro residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 663..677 FT /note="Polar residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT MOD_RES 120 FT /note="Phosphothreonine" FT /evidence="ECO:0007744|PubMed:23186163" FT MOD_RES 248 FT /note="Phosphothreonine" FT /evidence="ECO:0000250|UniProtKB:Q63801" FT MOD_RES 253 FT /note="Phosphotyrosine" FT /evidence="ECO:0000250|UniProtKB:Q63801" FT MOD_RES 264 FT /note="Phosphoserine" FT /evidence="ECO:0000250|UniProtKB:Q63801" FT MOD_RES 524 FT /note="Omega-N-methylarginine" FT /evidence="ECO:0007744|PubMed:24129315" FT MOD_RES 626 FT /note="Phosphoserine" FT /evidence="ECO:0000250|UniProtKB:Q62311" FT MOD_RES 634 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:23186163" FT MOD_RES 636 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:23186163" FT MOD_RES 653 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:16964243, FT ECO:0007744|PubMed:19690332, ECO:0007744|PubMed:23186163, FT ECO:0007744|PubMed:24275569" FT MOD_RES 660 FT /note="Phosphothreonine" FT /evidence="ECO:0007744|PubMed:16964243, FT ECO:0007744|PubMed:19690332, ECO:0007744|PubMed:23186163, FT ECO:0007744|PubMed:24275569" FT CROSSLNK 196 FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with FT G-Cter in SUMO2)" FT /evidence="ECO:0007744|PubMed:28112733" FT VAR_SEQ 1 FT /note="M -> MTKRRLQTITACLQLREGSPSLHRGLHPSREEKRDSRM (in FT isoform 3)" FT /evidence="ECO:0000303|PubMed:14702039" FT /id="VSP_043709" FT VAR_SEQ 43..52 FT /note="Missing (in isoform 4)" FT /evidence="ECO:0000269|PubMed:11583621" FT /id="VSP_059851" FT VAR_SEQ 477..486 FT /note="Missing (in isoform 2)" FT /evidence="ECO:0000303|PubMed:8262073" FT /id="VSP_037476" FT VARIANT 36 FT /note="C -> S (in dbSNP:rs4134897)" FT /evidence="ECO:0000269|Ref.5" FT /id="VAR_014349" FT VARIANT 46 FT /note="R -> C (in ALYUS; decreased interaction with TAF1 FT and TBP shown by functional expression studies in a FT Drosophila cell line; dbSNP:rs727503778)" FT /evidence="ECO:0000269|PubMed:25574841" FT /id="VAR_077840" FT VARIANT 71 FT /note="I -> T (in ALYUS; decreased interaction with TAF1, FT TAF9 and TBP shown by functional expression studies in a FT Drosophila cell line; dbSNP:rs374993554)" FT /evidence="ECO:0000269|PubMed:25558065, FT ECO:0000269|PubMed:25574841" FT /id="VAR_077841" FT CONFLICT 196 FT /note="K -> E (in Ref. 4; CAH10485)" FT /evidence="ECO:0000305" FT CONFLICT 417 FT /note="R -> W (in Ref. 4; CAH10485)" FT /evidence="ECO:0000305" FT HELIX 16..24 FT /evidence="ECO:0007829|PDB:6F3T" FT TURN 25..27 FT /evidence="ECO:0007829|PDB:6F3T" FT HELIX 33..60 FT /evidence="ECO:0007829|PDB:6F3T" FT STRAND 64..66 FT /evidence="ECO:0007829|PDB:6F3T" FT HELIX 68..78 FT /evidence="ECO:0007829|PDB:6F3T" FT HELIX 80..82 FT /evidence="ECO:0007829|PDB:7EGF" FT STRAND 83..87 FT /evidence="ECO:0007829|PDB:6F3T" FT STRAND 93..96 FT /evidence="ECO:0007829|PDB:7EGG" FT STRAND 104..106 FT /evidence="ECO:0007829|PDB:7EGF" FT STRAND 111..113 FT /evidence="ECO:0007829|PDB:7EGF" FT HELIX 116..119 FT /evidence="ECO:0007829|PDB:7EGG" FT HELIX 121..124 FT /evidence="ECO:0007829|PDB:7EGG" FT HELIX 127..129 FT /evidence="ECO:0007829|PDB:7EGG" FT STRAND 131..138 FT /evidence="ECO:0007829|PDB:7EGG" FT HELIX 209..212 FT /evidence="ECO:0007829|PDB:7EGH" FT HELIX 215..217 FT /evidence="ECO:0007829|PDB:7EGB" FT HELIX 218..230 FT /evidence="ECO:0007829|PDB:7EGH" FT STRAND 232..234 FT /evidence="ECO:0007829|PDB:7EGB" FT HELIX 236..248 FT /evidence="ECO:0007829|PDB:7EGH" FT HELIX 250..252 FT /evidence="ECO:0007829|PDB:7EGH" FT HELIX 256..269 FT /evidence="ECO:0007829|PDB:7EGH" FT TURN 271..274 FT /evidence="ECO:0007829|PDB:7EGH" FT HELIX 276..290 FT /evidence="ECO:0007829|PDB:7EGH" FT STRAND 293..295 FT /evidence="ECO:0007829|PDB:7EGH" FT HELIX 301..313 FT /evidence="ECO:0007829|PDB:7EGH" FT STRAND 320..322 FT /evidence="ECO:0007829|PDB:7EGH" FT HELIX 324..343 FT /evidence="ECO:0007829|PDB:7EGH" FT TURN 347..349 FT /evidence="ECO:0007829|PDB:7EGB" FT HELIX 352..363 FT /evidence="ECO:0007829|PDB:7EGH" FT STRAND 364..367 FT /evidence="ECO:0007829|PDB:7EGH" FT HELIX 370..381 FT /evidence="ECO:0007829|PDB:7EGH" FT HELIX 385..390 FT /evidence="ECO:0007829|PDB:7EGH" FT HELIX 393..395 FT /evidence="ECO:0007829|PDB:7EGH" FT HELIX 396..408 FT /evidence="ECO:0007829|PDB:7EGH" FT STRAND 413..415 FT /evidence="ECO:0007829|PDB:7EGH" FT HELIX 416..437 FT /evidence="ECO:0007829|PDB:7EGH" FT TURN 444..446 FT /evidence="ECO:0007829|PDB:7EGH" FT HELIX 447..451 FT /evidence="ECO:0007829|PDB:7EGH" FT TURN 452..454 FT /evidence="ECO:0007829|PDB:7EGB" FT HELIX 456..472 FT /evidence="ECO:0007829|PDB:7EGH" SQ SEQUENCE 677 AA; 72668 MW; 06C6BFA563580823 CRC64; MAEEKKLKLS NTVLPSESMK VVAESMGIAQ IQEETCQLLT DEVSYRIKEI AQDALKFMHM GKRQKLTTSD IDYALKLKNV EPLYGFHAQE FIPFRFASGG GRELYFYEEK EVDLSDIINT PLPRVPLDVC LKAHWLSIEG CQPAIPENPP PAPKEQQKAE ATEPLKSAKP GQEEDGPLKG KGQGATTADG KGKEKKAPPL LEGAPLRLKP RSIHELSVEQ QLYYKEITEA CVGSCEAKRA EALQSIATDP GLYQMLPRFS TFISEGVRVN VVQNNLALLI YLMRMVKALM DNPTLYLEKY VHELIPAVMT CIVSRQLCLR PDVDNHWALR DFAARLVAQI CKHFSTTTNN IQSRITKTFT KSWVDEKTPW TTRYGSIAGL AELGHDVIKT LILPRLQQEG ERIRSVLDGP VLSNIDRIGA DHVQSLLLKH CAPVLAKLRP PPDNQDAYRA EFGSLGPLLC SQVVKARAQA ALQAQQVNRT TLTITQPRPT LTLSQAPQPG PRTPGLLKVP GSIALPVQTL VSARAAAPPQ PSPPPTKFIV MSSSSSAPST QQVLSLSTSA PGSGSTTTSP VTTTVPSVQP IVKLVSTATT APPSTAPSGP GSVQKYIVVS LPPTGEGKGG PTSHPSPVPP PASSPSPLSG SALCGGKQEA GDSPPPAPGT PKANGSQPNS GSPQPAP //