TAF6_HUMAN
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 03-AUG-2022, entry version 211.
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 BAP18, 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 -!- WEB RESOURCE: Name=NIEHS-SNPs;
CC URL="http://egp.gs.washington.edu/data/taf6/";
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 RefSeq; NP_001177344.1; NM_001190415.1. [P49848-3]
DR RefSeq; NP_005632.1; NM_005641.3. [P49848-1]
DR RefSeq; NP_647476.1; NM_139315.2. [P49848-1]
DR RefSeq; XP_006716163.1; XM_006716100.2.
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 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 AlphaFoldDB; P49848; -.
DR SMR; P49848; -.
DR BioGRID; 112741; 113.
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 IntAct; P49848; 51.
DR MINT; P49848; -.
DR STRING; 9606.ENSP00000399982; -.
DR GlyGen; P49848; 15 sites, 2 O-linked glycans (15 sites).
DR iPTMnet; P49848; -.
DR MetOSite; P49848; -.
DR PhosphoSitePlus; P49848; -.
DR BioMuta; TAF6; -.
DR DMDM; 1729810; -.
DR EPD; P49848; -.
DR jPOST; P49848; -.
DR MassIVE; P49848; -.
DR MaxQB; P49848; -.
DR PaxDb; P49848; -.
DR PeptideAtlas; P49848; -.
DR PRIDE; P49848; -.
DR ProteomicsDB; 56157; -. [P49848-1]
DR ProteomicsDB; 56158; -. [P49848-2]
DR ProteomicsDB; 56159; -. [P49848-3]
DR Antibodypedia; 1765; 206 antibodies from 23 providers.
DR DNASU; 6878; -.
DR Ensembl; ENST00000344095.8; ENSP00000344537.4; ENSG00000106290.16. [P49848-1]
DR Ensembl; ENST00000437822.6; ENSP00000399982.2; ENSG00000106290.16. [P49848-3]
DR Ensembl; ENST00000452041.5; ENSP00000416396.1; ENSG00000106290.16. [P49848-1]
DR Ensembl; ENST00000453269.7; ENSP00000389575.2; ENSG00000106290.16. [P49848-1]
DR Ensembl; ENST00000460673.3; ENSP00000427710.3; ENSG00000106290.16. [P49848-1]
DR Ensembl; ENST00000472509.6; ENSP00000419760.2; ENSG00000106290.16. [P49848-1]
DR Ensembl; ENST00000685280.1; ENSP00000510209.1; ENSG00000106290.16. [P49848-1]
DR Ensembl; ENST00000686172.1; ENSP00000510809.1; ENSG00000106290.16. [P49848-4]
DR Ensembl; ENST00000686580.1; ENSP00000510270.1; ENSG00000106290.16. [P49848-1]
DR Ensembl; ENST00000686777.1; ENSP00000510166.1; ENSG00000106290.16. [P49848-1]
DR Ensembl; ENST00000687137.1; ENSP00000508432.1; ENSG00000106290.16. [P49848-1]
DR Ensembl; ENST00000687151.1; ENSP00000508852.1; ENSG00000106290.16. [P49848-4]
DR Ensembl; ENST00000687410.1; ENSP00000509158.1; ENSG00000106290.16. [P49848-1]
DR Ensembl; ENST00000687447.1; ENSP00000510217.1; ENSG00000106290.16. [P49848-1]
DR Ensembl; ENST00000687672.1; ENSP00000509741.1; ENSG00000106290.16. [P49848-4]
DR Ensembl; ENST00000687969.1; ENSP00000508679.1; ENSG00000106290.16. [P49848-1]
DR Ensembl; ENST00000688343.1; ENSP00000508691.1; ENSG00000106290.16. [P49848-1]
DR Ensembl; ENST00000688498.1; ENSP00000510409.1; ENSG00000106290.16. [P49848-1]
DR Ensembl; ENST00000688640.1; ENSP00000509783.1; ENSG00000106290.16. [P49848-1]
DR Ensembl; ENST00000689754.1; ENSP00000509866.1; ENSG00000106290.16. [P49848-1]
DR Ensembl; ENST00000690367.1; ENSP00000509821.1; ENSG00000106290.16. [P49848-4]
DR Ensembl; ENST00000691010.1; ENSP00000509320.1; ENSG00000106290.16. [P49848-4]
DR Ensembl; ENST00000691370.1; ENSP00000509500.1; ENSG00000106290.16. [P49848-1]
DR Ensembl; ENST00000691681.1; ENSP00000509494.1; ENSG00000106290.16. [P49848-1]
DR Ensembl; ENST00000692408.1; ENSP00000508788.1; ENSG00000106290.16. [P49848-4]
DR Ensembl; ENST00000692466.1; ENSP00000509041.1; ENSG00000106290.16. [P49848-1]
DR Ensembl; ENST00000692927.1; ENSP00000509335.1; ENSG00000106290.16. [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 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 neXtProt; NX_P49848; -.
DR OpenTargets; ENSG00000106290; -.
DR PharmGKB; PA36315; -.
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; 384329at2759; -.
DR PhylomeDB; P49848; -.
DR TreeFam; TF313632; -.
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 BioGRID-ORCS; 6878; 699 hits in 1065 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 204 other tissues.
DR ExpressionAtlas; P49848; baseline and differential.
DR Genevisible; P49848; HS.
DR GO; GO:0005829; C:cytosol; IDA:HPA.
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:0006915; P:apoptotic process; IEA:UniProtKB-KW.
DR GO; GO:0006352; P:DNA-templated transcription, initiation; IDA:UniProtKB.
DR GO; GO:0043966; P:histone H3 acetylation; IDA:ComplexPortal.
DR GO; GO:0035521; P:monoubiquitinated histone deubiquitination; IDA:ComplexPortal.
DR GO; GO:0035522; P:monoubiquitinated histone H2A deubiquitination; IDA:ComplexPortal.
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:2001244; P:positive regulation of intrinsic apoptotic signaling pathway; IDA:UniProtKB.
DR GO; GO:0060261; P:positive regulation of transcription initiation from RNA polymerase II promoter; IDA:UniProtKB.
DR GO; GO:0045893; P:positive regulation of transcription, DNA-templated; IC:ComplexPortal.
DR GO; GO:0006468; P:protein phosphorylation; IDA:ComplexPortal.
DR GO; GO:0006282; P:regulation of DNA repair; IC: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 from RNA polymerase II promoter; IDA:UniProtKB.
DR CDD; cd08050; TAF6C; 1.
DR DisProt; DP01262; -.
DR Gene3D; 1.10.20.10; -; 1.
DR Gene3D; 1.25.40.770; -; 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; PTHR10221; 1.
DR Pfam; PF02969; TAF; 1.
DR Pfam; PF07571; TAF6_C; 1.
DR SMART; SM00803; TAF; 1.
DR SUPFAM; SSF47113; SSF47113; 1.
DR SUPFAM; SSF48371; SSF48371; 1.
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; Reference proteome; Transcription;
KW 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 159..176
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 537..574
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 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 STRAND 131..138
FT /evidence="ECO:0007829|PDB:7EGG"
FT HELIX 218..230
FT /evidence="ECO:0007829|PDB:7EGH"
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 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 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
