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 27-MAR-2024, entry version 192. 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 UBIQUITINATION BY TRIM26. RX PubMed=29203640; DOI=10.1128/mcb.00449-17; RA Nakagawa T., Hosogane M., Nakagawa M., Morohoshi A., Funayama R., RA Nakayama K.; RT "Transforming Growth Factor beta-Induced Proliferative Arrest Mediated by RT TRIM26-Dependent TAF7 Degradation and Its Antagonism by MYC."; RL Mol. Cell. Biol. 38:0-0(2018). RN [23] 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 [24] 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 [25] {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 -!- PTM: Ubiquitinated by TRIM26; leading to proteasomal degradation. CC {ECO:0000269|PubMed:29203640}. 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 PDB; 8GXQ; EM; 5.04 A; DG=1-349. DR PDB; 8GXS; EM; 4.16 A; DG=1-349. DR PDB; 8WAK; EM; 5.47 A; G=1-349. DR PDB; 8WAL; EM; 8.52 A; G=1-349. DR PDB; 8WAN; EM; 6.07 A; G=1-349. DR PDB; 8WAO; EM; 6.40 A; G=1-349. DR PDB; 8WAP; EM; 5.85 A; G=1-349. DR PDB; 8WAQ; EM; 6.29 A; G=1-349. DR PDB; 8WAR; EM; 7.20 A; G=1-349. DR PDB; 8WAS; EM; 6.13 A; G=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 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; -. DR AlphaFoldDB; Q15545; -. DR EMDB; EMD-31111; -. DR SMR; Q15545; -. DR BioGRID; 112742; 106. 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; 39. 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; 9606-ENSP00000312709; -. DR PeptideAtlas; Q15545; -. DR ProteomicsDB; 60627; -. DR Pumba; Q15545; -. DR Antibodypedia; 1826; 192 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 AGR; HGNC:11541; -. 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; QENEGAN; -. DR OrthoDB; 2878374at2759; -. 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; 615 hits in 1180 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 211 other cell types or tissues. DR ExpressionAtlas; Q15545; baseline and differential. 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; IDA:UniProt. 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:0030520; P:intracellular estrogen receptor signaling pathway; IEA:Ensembl. DR GO; GO:0042789; P:mRNA transcription by RNA polymerase II; IDA:ComplexPortal. DR GO; GO:0045892; P:negative regulation of DNA-templated transcription; IDA:UniProtKB. 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:0045893; P:positive regulation of DNA-templated transcription; NAS:ComplexPortal. 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 by RNA polymerase II; IDA:ComplexPortal. 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: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 at 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; TRANSCRIPTION INITIATION FACTOR TFIID 55 KD SUBUNIT-RELATED; 1. DR PANTHER; PTHR12228:SF6; TRANSCRIPTION INITIATION FACTOR TFIID SUBUNIT 7; 1. DR Pfam; PF04658; TAFII55_N; 1. DR SMART; SM01370; TAFII55_N; 1. DR Genevisible; Q15545; HS. PE 1: Evidence at protein level; KW 3D-structure; Coiled coil; Nucleus; Phosphoprotein; Reference proteome; KW Transcription; Transcription regulation; Ubl conjugation. 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 //