TAF7_HUMAN
ID TAF7_HUMAN Reviewed; 349 AA.
AC Q15545; B2RBV9; Q13036;
DT 15-JUL-1998, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1996, sequence version 1.
DT 03-AUG-2022, entry version 183.
DE RecName: Full=Transcription initiation factor TFIID subunit 7;
DE AltName: Full=RNA polymerase II TBP-associated factor subunit F;
DE AltName: Full=Transcription initiation factor TFIID 55 kDa subunit;
DE Short=TAF(II)55;
DE Short=TAFII-55;
DE Short=TAFII55 {ECO:0000303|PubMed:11340078, ECO:0000303|PubMed:7824954, ECO:0000303|PubMed:8702684};
GN Name=TAF7; Synonyms=TAF2F, TAFII55;
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], AND SUBUNIT.
RX PubMed=8702684; DOI=10.1074/jbc.271.33.19774;
RA Lavigne A.C., Mengus G., May M., Dubrowskaya V., Tora L., Davidson I.;
RT "Multiple interactions between hTAFII55 and other TFIID subunits.
RT Requirements for the formation of stable ternary complexes between hTAFII55
RT and the TATA-binding protein.";
RL J. Biol. Chem. 271:19774-19780(1996).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA], AND SUBUNIT.
RX PubMed=7824954; DOI=10.1126/science.7824954;
RA Chiang C.-M., Roeder R.G.;
RT "Cloning of an intrinsic human TFIID subunit that interacts with multiple
RT transcriptional activators.";
RL Science 267:531-536(1995).
RN [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=11340078; DOI=10.1074/jbc.m102875200;
RA Zhou T., Chiang C.-M.;
RT "The intronless and TATA-less human TAFII55 gene contains a functional
RT initiator and a downstream promoter element.";
RL J. Biol. Chem. 276:25503-25511(2001).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Brain;
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 [5]
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 [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Skin;
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 [7]
RP FUNCTION, AND SUBUNIT.
RX PubMed=10438527; DOI=10.1074/jbc.274.33.23480;
RA Wu S.Y., Thomas M.C., Hou S.Y., Likhite V., Chiang C.M.;
RT "Isolation of mouse TFIID and functional characterization of TBP and TFIID
RT in mediating estrogen receptor and chromatin transcription.";
RL J. Biol. Chem. 274:23480-23490(1999).
RN [8]
RP INTERACTION WITH TAF1.
RX PubMed=11592977; DOI=10.1073/pnas.211444798;
RA Gegonne A., Weissman J.D., Singer D.S.;
RT "TAFII55 binding to TAFII250 inhibits its acetyltransferase activity.";
RL Proc. Natl. Acad. Sci. U.S.A. 98:12432-12437(2001).
RN [9]
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 [10]
RP INTERACTION WITH CIITA.
RX PubMed=20937824; DOI=10.1074/jbc.m110.173864;
RA Devaiah B.N., Lu H., Gegonne A., Sercan Z., Zhang H., Clifford R.J.,
RA Lee M.P., Singer D.S.;
RT "Novel functions for TAF7, a regulator of TAF1-independent transcription.";
RL J. Biol. Chem. 285:38772-38780(2010).
RN [11]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-213, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=17081983; DOI=10.1016/j.cell.2006.09.026;
RA Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P., Mann M.;
RT "Global, in vivo, and site-specific phosphorylation dynamics in signaling
RT networks.";
RL Cell 127:635-648(2006).
RN [12]
RP MOTIF, AND MUTAGENESIS OF LYS-5.
RX PubMed=16415881; DOI=10.1038/nsmb1045;
RA Couture J.-F., Collazo E., Hauk G., Trievel R.C.;
RT "Structural basis for the methylation site specificity of SET7/9.";
RL Nat. Struct. Mol. Biol. 13:140-146(2006).
RN [13]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=18691976; DOI=10.1016/j.molcel.2008.07.007;
RA Daub H., Olsen J.V., Bairlein M., Gnad F., Oppermann F.S., Korner R.,
RA Greff Z., Keri G., Stemmann O., Mann M.;
RT "Kinase-selective enrichment enables quantitative phosphoproteomics of the
RT kinome across the cell cycle.";
RL Mol. Cell 31:438-448(2008).
RN [14]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-171 AND SER-264, AND
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 [15]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-264, AND IDENTIFICATION BY
RP 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 [16]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-264, AND IDENTIFICATION BY
RP 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 [17]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-264, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21406692; DOI=10.1126/scisignal.2001570;
RA Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J., Johansen P.T.,
RA Kratchmarova I., Kassem M., Mann M., Olsen J.V., Blagoev B.;
RT "System-wide temporal characterization of the proteome and phosphoproteome
RT of human embryonic stem cell differentiation.";
RL Sci. Signal. 4:RS3-RS3(2011).
RN [18]
RP INTERACTION WITH TAF1, MISCELLANEOUS, PHOSPHORYLATION AT SER-264, AND
RP MUTAGENESIS OF SER-264.
RX PubMed=22711989; DOI=10.1128/mcb.00416-12;
RA Kloet S.L., Whiting J.L., Gafken P., Ranish J., Wang E.H.;
RT "Phosphorylation-dependent regulation of cyclin D1 and cyclin A gene
RT transcription by TFIID subunits TAF1 and TAF7.";
RL Mol. Cell. Biol. 32:3358-3369(2012).
RN [19]
RP PHOSPHORYLATION BY CIITA.
RX PubMed=24036077; DOI=10.1016/j.bbagrm.2013.09.001;
RA Soe K.C., Devaiah B.N., Singer D.S.;
RT "Transcriptional coactivator CIITA, a functional homolog of TAF1, has
RT kinase activity.";
RL Biochim. Biophys. Acta 1829:1184-1190(2013).
RN [20]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-171; SER-200; SER-201;
RP SER-213 AND SER-264, 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 [21]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-171 AND SER-264, 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 [22]
RP X-RAY CRYSTALLOGRAPHY (2.30 ANGSTROMS) IN COMPLEX WITH TAF1.
RX PubMed=25412659; DOI=10.1038/cr.2014.148;
RA Wang H., Curran E.C., Hinds T.R., Wang E.H., Zheng N.;
RT "Crystal structure of a TAF1-TAF7 complex in human transcription factor IID
RT reveals a promoter binding module.";
RL Cell Res. 24:1433-1444(2014).
RN [23]
RP STRUCTURE BY ELECTRON MICROSCOPY (8.50 ANGSTROMS), AND SUBUNIT.
RX PubMed=27007846; DOI=10.1038/nature17394;
RA Louder R.K., He Y., Lopez-Blanco J.R., Fang J., Chacon P., Nogales E.;
RT "Structure of promoter-bound TFIID and model of human pre-initiation
RT complex assembly.";
RL Nature 531:604-609(2016).
RN [24] {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:7EGH}
RP STRUCTURE BY ELECTRON MICROSCOPY (3.04 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,
CC PubMed:10438527). TAF7 forms a promoter DNA binding subcomplex of
CC TFIID, together with TAF1 and TAF2 (PubMed:33795473). Part of a TFIID
CC complex containing TAF10 (TFIID alpha) and a TFIID complex lacking
CC TAF10 (TFIID beta) (PubMed:10438527). {ECO:0000269|PubMed:10438527,
CC ECO:0000269|PubMed:33795473}.
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:10438527,
CC PubMed:27007846, PubMed:33795473). Part of a TFIID-containing RNA
CC polymerase II pre-initiation complex that is composed of TBP and at
CC least GTF2A1, GTF2A2, GTF2E1, GTF2E2, GTF2F1, GTF2H2, GTF2H3, GTF2H4,
CC GTF2H5, GTF2B, TCEA1, ERCC2, ERCC3, TAF1, TAF2, TAF3, TAF4, TAF5, TAF6,
CC TAF7, TAF8, TAF9, TAF10, TAF11, TAF12 and TAF13 (PubMed:27007846,
CC PubMed:33795473). Interacts with TAF1; the interaction is direct
CC (PubMed:25412659). Interacts with TAF1, TAF5, TAF11, TAF12, and TAF13,
CC but not with TAF10 or TBP (PubMed:10438527, PubMed:8702684). Component
CC of 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). Interacts with CIITA and TAF1 and inhibits their
CC acetyltransferase activity, and behaving as a repressor of CIITA- and
CC TAF1-regulated promoters (PubMed:20937824, PubMed:11592977).
CC {ECO:0000269|PubMed:10438527, ECO:0000269|PubMed:11592977,
CC ECO:0000269|PubMed:15960975, ECO:0000269|PubMed:20937824,
CC ECO:0000269|PubMed:25412659, ECO:0000269|PubMed:27007846,
CC ECO:0000269|PubMed:33795473, ECO:0000269|PubMed:8702684}.
CC -!- INTERACTION:
CC Q15545; Q6P4D5-2: PABIR3; NbExp=3; IntAct=EBI-1560194, EBI-9091052;
CC Q15545; Q03403: TFF2; NbExp=3; IntAct=EBI-1560194, EBI-4314702;
CC Q15545; P13051-2: UNG; NbExp=3; IntAct=EBI-1560194, EBI-25834258;
CC Q15545; Q80UV9-1: Taf1; Xeno; NbExp=2; IntAct=EBI-1560194, EBI-15563115;
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:Q9R1C0}.
CC -!- TISSUE SPECIFICITY: Ubiquitous.
CC -!- DOMAIN: The [KR]-[STA]-K motif is specifically recognized by the SETD7
CC methyltransferase, which methylates Lys-5 in vitro. {ECO:0000250}.
CC -!- PTM: Phosphorylated by CIITA. Phosphorylation at Ser-264 by TAF1 in
CC early G1 phase disrupts binding to TAF1. {ECO:0000269|PubMed:22711989,
CC ECO:0000269|PubMed:24036077}.
CC -!- MISCELLANEOUS: Overexpression of TAF7 in HeLa cells inhibits cyclin D1
CC and cyclin A gene transcription and causes the cells to accumulate in
CC early S phase. In contrast, depletion of TAF7 from TFIID complexes by
CC siRNAs increases histone H3 acetylation at both cyclin promoters and
CC stimulates cyclins CCND1 and CCNA gene transcription.
CC -!- SIMILARITY: Belongs to the TAF7 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; X97999; CAA66636.1; -; mRNA.
DR EMBL; U18062; AAB60347.1; -; mRNA.
DR EMBL; AF349038; AAK30585.1; -; Genomic_DNA.
DR EMBL; AK314837; BAG37356.1; -; mRNA.
DR EMBL; CH471062; EAW61966.1; -; Genomic_DNA.
DR EMBL; BC032737; AAH32737.1; -; mRNA.
DR CCDS; CCDS4259.1; -.
DR PIR; I38904; I38904.
DR RefSeq; NP_005633.2; NM_005642.2.
DR PDB; 4RGW; X-ray; 2.30 A; B=1-349.
DR PDB; 5FUR; EM; 8.50 A; H=1-349.
DR PDB; 6MZL; EM; 23.00 A; J=1-349.
DR PDB; 6MZM; EM; 7.50 A; J=1-349.
DR PDB; 7EDX; EM; 4.50 A; G=1-349.
DR PDB; 7EG7; EM; 6.20 A; G=1-349.
DR PDB; 7EG8; EM; 7.40 A; G=1-349.
DR PDB; 7EG9; EM; 3.70 A; G=1-349.
DR PDB; 7EGA; EM; 4.10 A; G=1-349.
DR PDB; 7EGB; EM; 3.30 A; G=1-349.
DR PDB; 7EGC; EM; 3.90 A; G=1-349.
DR PDB; 7EGD; EM; 6.75 A; G=1-349.
DR PDB; 7EGE; EM; 9.00 A; G=1-349.
DR PDB; 7EGH; EM; 3.04 A; G=1-349.
DR PDB; 7EGI; EM; 9.82 A; G=1-349.
DR PDB; 7EGJ; EM; 8.64 A; G=1-349.
DR PDB; 7ENA; EM; 4.07 A; DG=1-349.
DR PDB; 7ENC; EM; 4.13 A; DG=1-349.
DR PDBsum; 4RGW; -.
DR PDBsum; 5FUR; -.
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; 7EGH; -.
DR PDBsum; 7EGI; -.
DR PDBsum; 7EGJ; -.
DR PDBsum; 7ENA; -.
DR PDBsum; 7ENC; -.
DR AlphaFoldDB; Q15545; -.
DR SMR; Q15545; -.
DR BioGRID; 112742; 77.
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; Q15545; -.
DR DIP; DIP-29047N; -.
DR IntAct; Q15545; 38.
DR MINT; Q15545; -.
DR STRING; 9606.ENSP00000312709; -.
DR iPTMnet; Q15545; -.
DR PhosphoSitePlus; Q15545; -.
DR BioMuta; TAF7; -.
DR DMDM; 3024690; -.
DR EPD; Q15545; -.
DR jPOST; Q15545; -.
DR MassIVE; Q15545; -.
DR MaxQB; Q15545; -.
DR PaxDb; Q15545; -.
DR PeptideAtlas; Q15545; -.
DR PRIDE; Q15545; -.
DR ProteomicsDB; 60627; -.
DR Antibodypedia; 1826; 181 antibodies from 27 providers.
DR DNASU; 6879; -.
DR Ensembl; ENST00000313368.8; ENSP00000312709.5; ENSG00000178913.9.
DR Ensembl; ENST00000624761.2; ENSP00000485510.2; ENSG00000178913.9.
DR GeneID; 6879; -.
DR KEGG; hsa:6879; -.
DR MANE-Select; ENST00000313368.8; ENSP00000312709.5; NM_005642.3; NP_005633.2.
DR UCSC; uc003ljg.4; human.
DR CTD; 6879; -.
DR DisGeNET; 6879; -.
DR GeneCards; TAF7; -.
DR HGNC; HGNC:11541; TAF7.
DR HPA; ENSG00000178913; Low tissue specificity.
DR MIM; 600573; gene.
DR neXtProt; NX_Q15545; -.
DR OpenTargets; ENSG00000178913; -.
DR PharmGKB; PA36316; -.
DR VEuPathDB; HostDB:ENSG00000178913; -.
DR eggNOG; KOG4011; Eukaryota.
DR GeneTree; ENSGT00940000160861; -.
DR HOGENOM; CLU_037860_0_1_1; -.
DR InParanoid; Q15545; -.
DR OMA; KTLQYPH; -.
DR OrthoDB; 1348389at2759; -.
DR PhylomeDB; Q15545; -.
DR TreeFam; TF313044; -.
DR PathwayCommons; Q15545; -.
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-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; Q15545; -.
DR SIGNOR; Q15545; -.
DR BioGRID-ORCS; 6879; 590 hits in 1090 CRISPR screens.
DR ChiTaRS; TAF7; human.
DR GeneWiki; TAF7; -.
DR GenomeRNAi; 6879; -.
DR Pharos; Q15545; Tbio.
DR PRO; PR:Q15545; -.
DR Proteomes; UP000005640; Chromosome 5.
DR RNAct; Q15545; protein.
DR Bgee; ENSG00000178913; Expressed in calcaneal tendon and 209 other tissues.
DR ExpressionAtlas; Q15545; baseline and differential.
DR Genevisible; Q15545; HS.
DR GO; GO:0005737; C:cytoplasm; IEA:Ensembl.
DR GO; GO:0001673; C:male germ cell nucleus; IEA:Ensembl.
DR GO; GO:0071339; C:MLL1 complex; IDA:UniProtKB.
DR GO; GO:0005654; C:nucleoplasm; TAS:Reactome.
DR GO; GO:0005634; C:nucleus; EXP:ComplexPortal.
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:0005667; C:transcription regulator complex; IPI:ParkinsonsUK-UCL.
DR GO; GO:0140297; F:DNA-binding transcription factor binding; IPI:UniProtKB.
DR GO; GO:0035035; F:histone acetyltransferase binding; IPI:UniProtKB.
DR GO; GO:0046966; F:nuclear thyroid hormone receptor binding; IPI:UniProtKB.
DR GO; GO:0042809; F:nuclear vitamin D receptor binding; IPI:UniProtKB.
DR GO; GO:0106140; F:P-TEFb complex binding; IDA:UniProtKB.
DR GO; GO:0046982; F:protein heterodimerization activity; IPI:ParkinsonsUK-UCL.
DR GO; GO:0016251; F:RNA polymerase II general transcription initiation factor activity; IDA:ParkinsonsUK-UCL.
DR GO; GO:0001097; F:TFIIH-class transcription factor complex binding; IDA:UniProtKB.
DR GO; GO:0000976; F:transcription cis-regulatory region binding; IDA:UniProtKB.
DR GO; GO:0006352; P:DNA-templated transcription, initiation; IDA:UniProtKB.
DR GO; GO:0043966; P:histone H3 acetylation; IDA:ComplexPortal.
DR GO; GO:0030520; P:intracellular estrogen receptor signaling pathway; IEA:Ensembl.
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:0035067; P:negative regulation of histone acetylation; IDA:UniProtKB.
DR GO; GO:0090241; P:negative regulation of histone H4 acetylation; IDA:CACAO.
DR GO; GO:0045344; P:negative regulation of MHC class I biosynthetic process; IDA:CACAO.
DR GO; GO:0045347; P:negative regulation of MHC class II biosynthetic process; IMP:CACAO.
DR GO; GO:0006469; P:negative regulation of protein kinase activity; IDA:UniProtKB.
DR GO; GO:0000122; P:negative regulation of transcription by RNA polymerase II; IDA:UniProtKB.
DR GO; GO:0045892; P:negative regulation of transcription, DNA-templated; IDA:UniProtKB.
DR GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; IDA:UniProtKB.
DR GO; GO:0060261; P:positive regulation of transcription initiation from RNA polymerase II promoter; IDA:ComplexPortal.
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:0000296; P:spermine transport; ISS:GO_Central.
DR GO; GO:0006366; P:transcription by RNA polymerase II; IDA:UniProtKB.
DR GO; GO:0006367; P:transcription initiation from RNA polymerase II promoter; IDA:UniProtKB.
DR CDD; cd08047; TAF7; 1.
DR InterPro; IPR037817; TAF7.
DR InterPro; IPR006751; TAFII55_prot_cons_reg.
DR PANTHER; PTHR12228; PTHR12228; 1.
DR Pfam; PF04658; TAFII55_N; 1.
DR SMART; SM01370; TAFII55_N; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Coiled coil; Nucleus; Phosphoprotein; Reference proteome;
KW Transcription; Transcription regulation.
FT CHAIN 1..349
FT /note="Transcription initiation factor TFIID subunit 7"
FT /id="PRO_0000118881"
FT REGION 105..126
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 186..212
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 227..247
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 328..349
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 244..349
FT /evidence="ECO:0000255"
FT MOTIF 3..5
FT /note="[KR]-[STA]-K motif"
FT MOD_RES 171
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:23186163, ECO:0007744|PubMed:24275569"
FT MOD_RES 200
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 201
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 213
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17081983,
FT ECO:0007744|PubMed:23186163"
FT MOD_RES 264
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:22711989,
FT ECO:0007744|PubMed:18669648, ECO:0007744|PubMed:19690332,
FT ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:21406692,
FT ECO:0007744|PubMed:23186163, ECO:0007744|PubMed:24275569"
FT VARIANT 178
FT /note="S -> R"
FT /id="VAR_005629"
FT MUTAGEN 5
FT /note="K->R: Abolishes methylation in vitro."
FT /evidence="ECO:0000269|PubMed:16415881"
FT MUTAGEN 264
FT /note="S->A: Reduced H3 acetylation and transcription at
FT target promoters."
FT /evidence="ECO:0000269|PubMed:22711989"
FT MUTAGEN 264
FT /note="S->D: 50% reduction in TAF1-binding, reduced
FT incorporation of TAF7 into TFIID complexes."
FT /evidence="ECO:0000269|PubMed:22711989"
FT CONFLICT 283
FT /note="K -> N (in Ref. 2; AAB60347)"
FT /evidence="ECO:0000305"
FT STRAND 14..19
FT /evidence="ECO:0007829|PDB:4RGW"
FT HELIX 22..34
FT /evidence="ECO:0007829|PDB:4RGW"
FT HELIX 39..42
FT /evidence="ECO:0007829|PDB:4RGW"
FT STRAND 43..47
FT /evidence="ECO:0007829|PDB:4RGW"
FT STRAND 51..58
FT /evidence="ECO:0007829|PDB:4RGW"
FT STRAND 61..101
FT /evidence="ECO:0007829|PDB:4RGW"
FT HELIX 138..140
FT /evidence="ECO:0007829|PDB:4RGW"
FT HELIX 143..146
FT /evidence="ECO:0007829|PDB:4RGW"
FT HELIX 162..175
FT /evidence="ECO:0007829|PDB:7EGH"
FT STRAND 179..183
FT /evidence="ECO:0007829|PDB:7EGH"
SQ SEQUENCE 349 AA; 40259 MW; 0AAFD3E33E3CCD6E CRC64;
MSKSKDDAPH ELESQFILRL PPEYASTVRR AVQSGHVNLK DRLTIELHPD GRHGIVRVDR
VPLASKLVDL PCVMESLKTI DKKTFYKTAD ICQMLVSTVD GDLYPPVEEP VASTDPKASK
KKDKDKEKKF IWNHGITLPL KNVRKRRFRK TAKKKYIESP DVEKEVKRLL STDAEAVSTR
WEIIAEDETK EAENQGLDIS SPGMSGHRQG HDSLEHDELR EIFNDLSSSS EDEDETQHQD
EEDINIIDTE EDLERQLQDK LNESDEQHQE NEGTNQLVMG IQKQIDNMKG KLQETQDRAK
RQEDLIMKVE NLALKNRFQA VLDELKQKED REKEQLSSLQ EELESLLEK
