T2FA_HUMAN
ID T2FA_HUMAN Reviewed; 517 AA.
AC P35269; B2RCS0; Q9BWN0;
DT 01-FEB-1994, integrated into UniProtKB/Swiss-Prot.
DT 13-APR-2004, sequence version 2.
DT 03-AUG-2022, entry version 213.
DE RecName: Full=General transcription factor IIF subunit 1;
DE AltName: Full=General transcription factor IIF 74 kDa subunit;
DE AltName: Full=Transcription initiation factor IIF subunit alpha;
DE Short=TFIIF-alpha;
DE AltName: Full=Transcription initiation factor RAP74;
GN Name=GTF2F1; Synonyms=RAP74;
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 PARTIAL PROTEIN SEQUENCE.
RX PubMed=1734283; DOI=10.1038/355461a0;
RA Aso T., Vasavada H.A., Kawaguchi T., Germino F.J., Ganguly S., Kitajima S.,
RA Weissman S.M., Yasukochi Y.;
RT "Characterization of cDNA for the large subunit of the transcription
RT initiation factor TFIIF.";
RL Nature 355:461-464(1992).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA], AND PARTIAL PROTEIN SEQUENCE.
RX PubMed=1734284; DOI=10.1038/355464a0;
RA Finkelstein A., Kostrub C.F., Li J., Chavez D.P., Wang B.Q., Fang S.M.,
RA Greenblatt J., Burton Z.F.;
RT "A cDNA encoding RAP74, a general initiation factor for transcription by
RT RNA polymerase II.";
RL Nature 355:464-467(1992).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RA Kalnine N., Chen X., Rolfs A., Halleck A., Hines L., Eisenstein S.,
RA Koundinya M., Raphael J., Moreira D., Kelley T., LaBaer J., Lin Y.,
RA Phelan M., Farmer A.;
RT "Cloning of human full-length CDSs in BD Creator(TM) system donor vector.";
RL Submitted (MAY-2003) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Stomach;
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=Eye, and Muscle;
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 INTERACTION WITH TAF6.
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 [8]
RP PHOSPHORYLATION AT SERINE RESIDUES.
RX PubMed=8625415; DOI=10.1016/s0092-8674(00)81055-7;
RA Dikstein R., Ruppert S., Tjian R.;
RT "TAFII250 is a bipartite protein kinase that phosphorylates the base
RT transcription factor RAP74.";
RL Cell 84:781-790(1996).
RN [9]
RP INTERACTION WITH GTF2B.
RX PubMed=8662660; DOI=10.1074/jbc.271.20.11703;
RA Fang S.M., Burton Z.F.;
RT "RNA polymerase II-associated protein (RAP) 74 binds transcription factor
RT (TF) IIB and blocks TFIIB-RAP30 binding.";
RL J. Biol. Chem. 271:11703-11709(1996).
RN [10]
RP FUNCTION, PHOSPHORYLATION AT SER-385 AND THR-389, AND MUTAGENESIS OF
RP SER-385 AND THR-389.
RX PubMed=10428810; DOI=10.1074/jbc.274.32.22387;
RA Rossignol M., Keriel A., Staub A., Egly J.-M.;
RT "Kinase activity and phosphorylation of the largest subunit of TFIIF
RT transcription factor.";
RL J. Biol. Chem. 274:22387-22392(1999).
RN [11]
RP INTERACTION WITH URI1.
RX PubMed=12737519; DOI=10.1038/sj.cr.7290155;
RA Wei W., Gu J.X., Zhu C.Q., Sun F.Y., Dorjsuren D., Lin Y., Murakami S.;
RT "Interaction with general transcription factor IIF (TFIIF) is required for
RT the suppression of activated transcription by RPB5-mediating protein
RT (RMP).";
RL Cell Res. 13:111-120(2003).
RN [12]
RP INTERACTION WITH GTF2B.
RX PubMed=12931194; DOI=10.1038/nature01899;
RA Choi C.H., Hiromura M., Usheva A.;
RT "Transcription factor IIB acetylates itself to regulate transcription.";
RL Nature 424:965-969(2003).
RN [13]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-217; SER-218; SER-221 AND
RP SER-224, AND IDENTIFICATION BY 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 [14]
RP INDUCTION, AND IDENTIFICATION BY MASS SPECTROMETRY.
RX PubMed=16548883; DOI=10.1111/j.1462-5822.2005.00644.x;
RA Leong W.F., Chow V.T.;
RT "Transcriptomic and proteomic analyses of rhabdomyosarcoma cells reveal
RT differential cellular gene expression in response to enterovirus 71
RT infection.";
RL Cell. Microbiol. 8:565-580(2006).
RN [15]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-433, AND IDENTIFICATION BY
RP 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 [16]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-377; SER-380; SER-381;
RP SER-385; THR-389; SER-431; SER-433; SER-436; THR-446 AND SER-449, 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 [17]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, CLEAVAGE OF INITIATOR
RP METHIONINE [LARGE SCALE ANALYSIS], AND IDENTIFICATION BY MASS SPECTROMETRY
RP [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 [18]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-217; SER-385 AND THR-389, 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 [19]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-407, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=19608861; DOI=10.1126/science.1175371;
RA Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T.C.,
RA Olsen J.V., Mann M.;
RT "Lysine acetylation targets protein complexes and co-regulates major
RT cellular functions.";
RL Science 325:834-840(2009).
RN [20]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-217; SER-218; SER-221;
RP SER-224 AND SER-433, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE
RP 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 [21]
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 [22]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-217; SER-218; SER-224;
RP THR-331; SER-385 AND SER-391, AND IDENTIFICATION BY MASS SPECTROMETRY
RP [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 [23]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, CLEAVAGE OF INITIATOR
RP METHIONINE [LARGE SCALE ANALYSIS], AND IDENTIFICATION BY MASS SPECTROMETRY
RP [LARGE SCALE ANALYSIS].
RX PubMed=22223895; DOI=10.1074/mcp.m111.015131;
RA Bienvenut W.V., Sumpton D., Martinez A., Lilla S., Espagne C., Meinnel T.,
RA Giglione C.;
RT "Comparative large-scale characterisation of plant vs. mammal proteins
RT reveals similar and idiosyncratic N-alpha acetylation features.";
RL Mol. Cell. Proteomics 11:M111.015131-M111.015131(2012).
RN [24]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, CLEAVAGE OF INITIATOR
RP METHIONINE [LARGE SCALE ANALYSIS], AND IDENTIFICATION BY MASS SPECTROMETRY
RP [LARGE SCALE ANALYSIS].
RX PubMed=22814378; DOI=10.1073/pnas.1210303109;
RA Van Damme P., Lasa M., Polevoda B., Gazquez C., Elosegui-Artola A.,
RA Kim D.S., De Juan-Pardo E., Demeyer K., Hole K., Larrea E., Timmerman E.,
RA Prieto J., Arnesen T., Sherman F., Gevaert K., Aldabe R.;
RT "N-terminal acetylome analyses and functional insights of the N-terminal
RT acetyltransferase NatB.";
RL Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012).
RN [25]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-156; SER-377; SER-385;
RP THR-389; SER-431; SER-433 AND THR-437, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE 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 [26]
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 [27]
RP X-RAY CRYSTALLOGRAPHY (1.7 ANGSTROMS) OF 5-153 IN COMPLEX WITH GTF2F2.
RX PubMed=11183778; DOI=10.1006/jmbi.2000.4110;
RA Gaiser F., Tan S., Richmond T.J.;
RT "Novel dimerization fold of RAP30/RAP74 in human TFIIF at 1.7 A
RT resolution.";
RL J. Mol. Biol. 302:1119-1127(2000).
RN [28]
RP X-RAY CRYSTALLOGRAPHY (1.02 ANGSTROMS) OF 451-517.
RX PubMed=11248041; DOI=10.1073/pnas.051631098;
RA Kamada K., De Angelis J., Roeder R.G., Burley S.K.;
RT "Crystal structure of the C-terminal domain of the RAP74 subunit of human
RT transcription factor IIF.";
RL Proc. Natl. Acad. Sci. U.S.A. 98:3115-3120(2001).
RN [29]
RP X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS) OF 449-517 IN COMPLEX WITH CTDP1.
RX PubMed=12591941; DOI=10.1073/pnas.262798199;
RA Kamada K., Roeder R.G., Burley S.K.;
RT "Molecular mechanism of recruitment of TFIIF-associating RNA polymerase C-
RT terminal domain phosphatase (FCP1) by transcription factor IIF.";
RL Proc. Natl. Acad. Sci. U.S.A. 100:2296-2299(2003).
RN [30]
RP STRUCTURE BY NMR OF 451-517.
RX PubMed=12578358; DOI=10.1021/bi0265473;
RA Nguyen B.D., Chen H.T., Kobor M.S., Greenblatt J., Legault P.,
RA Omichinski J.G.;
RT "Solution structure of the carboxyl-terminal domain of RAP74 and NMR
RT characterization of the FCP1-binding sites of RAP74 and human TFIIB.";
RL Biochemistry 42:1460-1469(2003).
RN [31]
RP STRUCTURE BY NMR OF 451-517.
RX PubMed=12732728; DOI=10.1073/pnas.1031524100;
RA Nguyen B.D., Abbott K.L., Potempa K., Kobor M.S., Archambault J.,
RA Greenblatt J., Legault P., Omichinski J.G.;
RT "NMR structure of a complex containing the TFIIF subunit RAP74 and the RNA
RT polymerase II carboxyl-terminal domain phosphatase FCP1.";
RL Proc. Natl. Acad. Sci. U.S.A. 100:5688-5693(2003).
CC -!- FUNCTION: TFIIF is a general transcription initiation factor that binds
CC to RNA polymerase II and helps to recruit it to the initiation complex
CC in collaboration with TFIIB. It promotes transcription elongation.
CC {ECO:0000269|PubMed:10428810}.
CC -!- SUBUNIT: Heterodimer of an alpha and a beta subunit. Interacts with
CC GTF2F2, CTDP1, TAF6/TAFII80 and URI1. Interacts with GTF2B (via C-
CC terminus and preferentially via acetylated form); this interaction
CC prevents binding of GTF2B to GTF2F2 (PubMed:8662660, PubMed:12931194).
CC {ECO:0000269|PubMed:11183778, ECO:0000269|PubMed:12591941,
CC ECO:0000269|PubMed:12737519, ECO:0000269|PubMed:12931194,
CC ECO:0000269|PubMed:7667268, ECO:0000269|PubMed:8662660}.
CC -!- INTERACTION:
CC P35269; Q9Y5B0: CTDP1; NbExp=2; IntAct=EBI-457886, EBI-2807555;
CC P35269; P13984: GTF2F2; NbExp=16; IntAct=EBI-457886, EBI-1030560;
CC P35269; P11831: SRF; NbExp=2; IntAct=EBI-457886, EBI-493034;
CC P35269; P21675: TAF1; NbExp=3; IntAct=EBI-457886, EBI-491289;
CC P35269; O94763: URI1; NbExp=3; IntAct=EBI-457886, EBI-357067;
CC -!- SUBCELLULAR LOCATION: Nucleus.
CC -!- INDUCTION: Up-regulated in response to enterovirus 71 (EV71) infection.
CC {ECO:0000269|PubMed:16548883}.
CC -!- PTM: Phosphorylated on Ser and other residues by TAF1 and casein kinase
CC II-like kinases. {ECO:0000269|PubMed:10428810,
CC ECO:0000269|PubMed:8625415}.
CC -!- SIMILARITY: Belongs to the TFIIF alpha subunit family. {ECO:0000305}.
CC -!- CAUTION: Was reported to have a protein kinase activity and to
CC autophosphorylates on Ser-385 and Thr-389.
CC {ECO:0000305|PubMed:10428810}.
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DR EMBL; X64037; CAA45408.1; -; mRNA.
DR EMBL; X64002; CAA45404.1; -; mRNA.
DR EMBL; BT007097; AAP35761.1; -; mRNA.
DR EMBL; AK315240; BAG37667.1; -; mRNA.
DR EMBL; CH471139; EAW69098.1; -; Genomic_DNA.
DR EMBL; BC000120; AAH00120.1; -; mRNA.
DR EMBL; BC013007; AAH13007.1; -; mRNA.
DR CCDS; CCDS12165.1; -.
DR PIR; S20248; S20248.
DR RefSeq; NP_002087.2; NM_002096.2.
DR PDB; 1F3U; X-ray; 1.70 A; B/D/F/H=2-172.
DR PDB; 1I27; X-ray; 1.02 A; A=449-517.
DR PDB; 1J2X; X-ray; 2.00 A; A=449-517.
DR PDB; 1NHA; NMR; -; A=436-517.
DR PDB; 1ONV; NMR; -; A=436-517.
DR PDB; 2K7L; NMR; -; A=451-517.
DR PDB; 5IY6; EM; 7.20 A; S=1-517.
DR PDB; 5IY7; EM; 8.60 A; S=1-517.
DR PDB; 5IY8; EM; 7.90 A; S=1-517.
DR PDB; 5IY9; EM; 6.30 A; S=1-517.
DR PDB; 5IYA; EM; 5.40 A; S=1-517.
DR PDB; 5IYB; EM; 3.90 A; S=1-517.
DR PDB; 5IYC; EM; 3.90 A; S=1-517.
DR PDB; 5IYD; EM; 3.90 A; S=1-517.
DR PDB; 6O9L; EM; 7.20 A; S=1-517.
DR PDB; 7EDX; EM; 4.50 A; S=1-517.
DR PDB; 7EG7; EM; 6.20 A; S=1-517.
DR PDB; 7EG8; EM; 7.40 A; S=1-517.
DR PDB; 7EG9; EM; 3.70 A; S=1-517.
DR PDB; 7EGA; EM; 4.10 A; S=1-517.
DR PDB; 7EGB; EM; 3.30 A; S=1-517.
DR PDB; 7EGC; EM; 3.90 A; S=1-517.
DR PDB; 7ENA; EM; 4.07 A; FA=1-517.
DR PDB; 7ENC; EM; 4.13 A; FA=1-517.
DR PDB; 7LBM; EM; 4.80 A; S=1-517.
DR PDB; 7NVR; EM; 4.50 A; Q=1-517.
DR PDB; 7NVS; EM; 2.80 A; Q=1-517.
DR PDB; 7NVT; EM; 2.90 A; Q=1-517.
DR PDB; 7NVU; EM; 2.50 A; Q=1-517.
DR PDB; 7NVY; EM; 7.30 A; Q=1-517.
DR PDB; 7NVZ; EM; 7.20 A; Q=1-517.
DR PDB; 7NW0; EM; 6.60 A; Q=1-517.
DR PDBsum; 1F3U; -.
DR PDBsum; 1I27; -.
DR PDBsum; 1J2X; -.
DR PDBsum; 1NHA; -.
DR PDBsum; 1ONV; -.
DR PDBsum; 2K7L; -.
DR PDBsum; 5IY6; -.
DR PDBsum; 5IY7; -.
DR PDBsum; 5IY8; -.
DR PDBsum; 5IY9; -.
DR PDBsum; 5IYA; -.
DR PDBsum; 5IYB; -.
DR PDBsum; 5IYC; -.
DR PDBsum; 5IYD; -.
DR PDBsum; 6O9L; -.
DR PDBsum; 7EDX; -.
DR PDBsum; 7EG7; -.
DR PDBsum; 7EG8; -.
DR PDBsum; 7EG9; -.
DR PDBsum; 7EGA; -.
DR PDBsum; 7EGB; -.
DR PDBsum; 7EGC; -.
DR PDBsum; 7ENA; -.
DR PDBsum; 7ENC; -.
DR PDBsum; 7LBM; -.
DR PDBsum; 7NVR; -.
DR PDBsum; 7NVS; -.
DR PDBsum; 7NVT; -.
DR PDBsum; 7NVU; -.
DR PDBsum; 7NVY; -.
DR PDBsum; 7NVZ; -.
DR PDBsum; 7NW0; -.
DR AlphaFoldDB; P35269; -.
DR BMRB; P35269; -.
DR SMR; P35269; -.
DR BioGRID; 109217; 159.
DR ComplexPortal; CPX-79; Transcription factor TFIIF complex.
DR CORUM; P35269; -.
DR DIP; DIP-677N; -.
DR IntAct; P35269; 60.
DR MINT; P35269; -.
DR STRING; 9606.ENSP00000377969; -.
DR GlyGen; P35269; 1 site, 1 O-linked glycan (1 site).
DR iPTMnet; P35269; -.
DR MetOSite; P35269; -.
DR PhosphoSitePlus; P35269; -.
DR BioMuta; GTF2F1; -.
DR DMDM; 46397744; -.
DR EPD; P35269; -.
DR jPOST; P35269; -.
DR MassIVE; P35269; -.
DR MaxQB; P35269; -.
DR PaxDb; P35269; -.
DR PeptideAtlas; P35269; -.
DR PRIDE; P35269; -.
DR ProteomicsDB; 55019; -.
DR TopDownProteomics; P35269; -.
DR Antibodypedia; 11855; 306 antibodies from 27 providers.
DR DNASU; 2962; -.
DR Ensembl; ENST00000394456.10; ENSP00000377969.3; ENSG00000125651.14.
DR GeneID; 2962; -.
DR KEGG; hsa:2962; -.
DR MANE-Select; ENST00000394456.10; ENSP00000377969.3; NM_002096.3; NP_002087.2.
DR UCSC; uc002meq.3; human.
DR CTD; 2962; -.
DR DisGeNET; 2962; -.
DR GeneCards; GTF2F1; -.
DR HGNC; HGNC:4652; GTF2F1.
DR HPA; ENSG00000125651; Low tissue specificity.
DR MIM; 189968; gene.
DR neXtProt; NX_P35269; -.
DR OpenTargets; ENSG00000125651; -.
DR PharmGKB; PA29038; -.
DR VEuPathDB; HostDB:ENSG00000125651; -.
DR eggNOG; KOG2393; Eukaryota.
DR GeneTree; ENSGT00440000038032; -.
DR HOGENOM; CLU_027572_2_0_1; -.
DR InParanoid; P35269; -.
DR OMA; NNMKEFR; -.
DR OrthoDB; 893557at2759; -.
DR PhylomeDB; P35269; -.
DR TreeFam; TF313850; -.
DR PathwayCommons; P35269; -.
DR Reactome; R-HSA-112382; Formation of RNA Pol II elongation complex.
DR Reactome; R-HSA-113418; Formation of the Early Elongation Complex.
DR Reactome; R-HSA-167152; Formation of HIV elongation complex in the absence of HIV Tat.
DR Reactome; R-HSA-167158; Formation of the HIV-1 Early Elongation Complex.
DR Reactome; R-HSA-167160; RNA Pol II CTD phosphorylation and interaction with CE during HIV infection.
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-167200; Formation of HIV-1 elongation complex containing HIV-1 Tat.
DR Reactome; R-HSA-167238; Pausing and recovery of Tat-mediated HIV elongation.
DR Reactome; R-HSA-167242; Abortive elongation of HIV-1 transcript in the absence of Tat.
DR Reactome; R-HSA-167243; Tat-mediated HIV elongation arrest and recovery.
DR Reactome; R-HSA-167246; Tat-mediated elongation of the HIV-1 transcript.
DR Reactome; R-HSA-167287; HIV elongation arrest and recovery.
DR Reactome; R-HSA-167290; Pausing and recovery of HIV elongation.
DR Reactome; R-HSA-168325; Viral Messenger RNA Synthesis.
DR Reactome; R-HSA-674695; RNA Polymerase II Pre-transcription Events.
DR Reactome; R-HSA-6796648; TP53 Regulates Transcription of DNA Repair Genes.
DR Reactome; R-HSA-6803529; FGFR2 alternative splicing.
DR Reactome; R-HSA-6807505; RNA polymerase II transcribes snRNA genes.
DR Reactome; R-HSA-72086; mRNA Capping.
DR Reactome; R-HSA-72163; mRNA Splicing - Major Pathway.
DR Reactome; R-HSA-72165; mRNA Splicing - Minor Pathway.
DR Reactome; R-HSA-72203; Processing of Capped Intron-Containing Pre-mRNA.
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-75955; RNA Polymerase II Transcription Elongation.
DR Reactome; R-HSA-76042; RNA Polymerase II Transcription Initiation And Promoter Clearance.
DR Reactome; R-HSA-77075; RNA Pol II CTD phosphorylation and interaction with CE.
DR Reactome; R-HSA-8851708; Signaling by FGFR2 IIIa TM.
DR Reactome; R-HSA-9018519; Estrogen-dependent gene expression.
DR SignaLink; P35269; -.
DR SIGNOR; P35269; -.
DR BioGRID-ORCS; 2962; 360 hits in 1087 CRISPR screens.
DR ChiTaRS; GTF2F1; human.
DR EvolutionaryTrace; P35269; -.
DR GeneWiki; GTF2F1; -.
DR GenomeRNAi; 2962; -.
DR Pharos; P35269; Tbio.
DR PRO; PR:P35269; -.
DR Proteomes; UP000005640; Chromosome 19.
DR RNAct; P35269; protein.
DR Bgee; ENSG00000125651; Expressed in cerebellum and 99 other tissues.
DR ExpressionAtlas; P35269; baseline and differential.
DR Genevisible; P35269; HS.
DR GO; GO:0030054; C:cell junction; IDA:HPA.
DR GO; GO:0043231; C:intracellular membrane-bounded organelle; IDA:HPA.
DR GO; GO:0005654; C:nucleoplasm; IDA:HPA.
DR GO; GO:0005634; C:nucleus; IMP:CAFA.
DR GO; GO:0032991; C:protein-containing complex; IMP:CAFA.
DR GO; GO:0005669; C:transcription factor TFIID complex; IDA:UniProtKB.
DR GO; GO:0005674; C:transcription factor TFIIF complex; IPI:ComplexPortal.
DR GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
DR GO; GO:0019211; F:phosphatase activator activity; IDA:UniProtKB.
DR GO; GO:1990841; F:promoter-specific chromatin binding; IDA:UniProtKB.
DR GO; GO:0019904; F:protein domain specific binding; IPI:CAFA.
DR GO; GO:0019903; F:protein phosphatase binding; IPI:CAFA.
DR GO; GO:0003723; F:RNA binding; HDA:UniProtKB.
DR GO; GO:0016251; F:RNA polymerase II general transcription initiation factor activity; IDA:ARUK-UCL.
DR GO; GO:0001091; F:RNA polymerase II general transcription initiation factor binding; IPI:BHF-UCL.
DR GO; GO:0001096; F:TFIIF-class transcription factor complex binding; IBA:GO_Central.
DR GO; GO:0032091; P:negative regulation of protein binding; IMP:UniProtKB.
DR GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; IDA:ComplexPortal.
DR GO; GO:0032968; P:positive regulation of transcription elongation from RNA polymerase II promoter; IEA:InterPro.
DR GO; GO:0009615; P:response to virus; IEP:UniProtKB.
DR GO; GO:0006366; P:transcription by RNA polymerase II; TAS:ProtInc.
DR GO; GO:0006368; P:transcription elongation from RNA polymerase II promoter; IDA:ComplexPortal.
DR GO; GO:0006367; P:transcription initiation from RNA polymerase II promoter; IDA:ARUK-UCL.
DR DisProt; DP03035; -.
DR Gene3D; 1.10.10.10; -; 1.
DR IDEAL; IID00369; -.
DR InterPro; IPR008851; TFIIF-alpha.
DR InterPro; IPR011039; TFIIF_interaction.
DR InterPro; IPR036388; WH-like_DNA-bd_sf.
DR InterPro; IPR036390; WH_DNA-bd_sf.
DR PANTHER; PTHR13011; PTHR13011; 1.
DR Pfam; PF05793; TFIIF_alpha; 1.
DR SUPFAM; SSF46785; SSF46785; 1.
DR SUPFAM; SSF50916; SSF50916; 2.
PE 1: Evidence at protein level;
KW 3D-structure; Acetylation; Direct protein sequencing; DNA-binding; Nucleus;
KW Phosphoprotein; Reference proteome; Transcription;
KW Transcription regulation.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0007744|PubMed:19413330,
FT ECO:0007744|PubMed:22223895, ECO:0007744|PubMed:22814378"
FT CHAIN 2..517
FT /note="General transcription factor IIF subunit 1"
FT /id="PRO_0000211231"
FT REGION 178..466
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 179..214
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 273..287
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 288..305
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 306..320
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 321..345
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 380..405
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 429..453
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 2
FT /note="N-acetylalanine"
FT /evidence="ECO:0007744|PubMed:19413330,
FT ECO:0007744|PubMed:22223895, ECO:0007744|PubMed:22814378"
FT MOD_RES 156
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 217
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17081983,
FT ECO:0007744|PubMed:19690332, ECO:0007744|PubMed:20068231,
FT ECO:0007744|PubMed:21406692"
FT MOD_RES 218
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17081983,
FT ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:21406692"
FT MOD_RES 221
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17081983,
FT ECO:0007744|PubMed:20068231"
FT MOD_RES 224
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17081983,
FT ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:21406692"
FT MOD_RES 331
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:21406692"
FT MOD_RES 377
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:23186163"
FT MOD_RES 380
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648"
FT MOD_RES 381
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648"
FT MOD_RES 385
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:10428810,
FT ECO:0007744|PubMed:18669648, ECO:0007744|PubMed:19690332,
FT ECO:0007744|PubMed:21406692, ECO:0007744|PubMed:23186163"
FT MOD_RES 389
FT /note="Phosphothreonine"
FT /evidence="ECO:0000269|PubMed:10428810,
FT ECO:0007744|PubMed:18669648, ECO:0007744|PubMed:19690332,
FT ECO:0007744|PubMed:23186163"
FT MOD_RES 391
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21406692"
FT MOD_RES 407
FT /note="N6-acetyllysine"
FT /evidence="ECO:0007744|PubMed:19608861"
FT MOD_RES 431
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:23186163"
FT MOD_RES 433
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:16964243,
FT ECO:0007744|PubMed:18669648, ECO:0007744|PubMed:20068231,
FT ECO:0007744|PubMed:23186163"
FT MOD_RES 436
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648"
FT MOD_RES 437
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 446
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:18669648"
FT MOD_RES 449
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648"
FT VARIANT 3
FT /note="A -> V (in dbSNP:rs34826931)"
FT /id="VAR_039004"
FT MUTAGEN 385
FT /note="S->A: Eliminates putative kinase activity; when
FT associated with A-389."
FT /evidence="ECO:0000269|PubMed:10428810"
FT MUTAGEN 389
FT /note="T->A: Eliminates putative kinase activity; when
FT associated with A-385."
FT /evidence="ECO:0000269|PubMed:10428810"
FT CONFLICT 231
FT /note="V -> I (in Ref. 2; CAA45404)"
FT /evidence="ECO:0000305"
FT CONFLICT 361
FT /note="L -> F (in Ref. 1; CAA45408)"
FT /evidence="ECO:0000305"
FT HELIX 6..9
FT /evidence="ECO:0007829|PDB:7NVU"
FT STRAND 10..17
FT /evidence="ECO:0007829|PDB:1F3U"
FT STRAND 23..31
FT /evidence="ECO:0007829|PDB:1F3U"
FT HELIX 33..35
FT /evidence="ECO:0007829|PDB:1F3U"
FT HELIX 39..41
FT /evidence="ECO:0007829|PDB:1F3U"
FT STRAND 45..49
FT /evidence="ECO:0007829|PDB:1F3U"
FT HELIX 52..55
FT /evidence="ECO:0007829|PDB:1F3U"
FT STRAND 58..61
FT /evidence="ECO:0007829|PDB:1F3U"
FT HELIX 76..78
FT /evidence="ECO:0007829|PDB:1F3U"
FT STRAND 84..87
FT /evidence="ECO:0007829|PDB:1F3U"
FT STRAND 98..104
FT /evidence="ECO:0007829|PDB:1F3U"
FT STRAND 109..114
FT /evidence="ECO:0007829|PDB:1F3U"
FT STRAND 120..129
FT /evidence="ECO:0007829|PDB:1F3U"
FT STRAND 135..148
FT /evidence="ECO:0007829|PDB:1F3U"
FT HELIX 149..151
FT /evidence="ECO:0007829|PDB:1F3U"
FT HELIX 157..167
FT /evidence="ECO:0007829|PDB:1F3U"
FT HELIX 175..179
FT /evidence="ECO:0007829|PDB:7NVU"
FT HELIX 456..465
FT /evidence="ECO:0007829|PDB:1I27"
FT HELIX 470..475
FT /evidence="ECO:0007829|PDB:1I27"
FT HELIX 479..482
FT /evidence="ECO:0007829|PDB:1I27"
FT HELIX 486..500
FT /evidence="ECO:0007829|PDB:1I27"
FT STRAND 503..507
FT /evidence="ECO:0007829|PDB:1I27"
FT STRAND 510..515
FT /evidence="ECO:0007829|PDB:1I27"
SQ SEQUENCE 517 AA; 58240 MW; 1032B04A36BDC24F CRC64;
MAALGPSSQN VTEYVVRVPK NTTKKYNIMA FNAADKVNFA TWNQARLERD LSNKKIYQEE
EMPESGAGSE FNRKLREEAR RKKYGIVLKE FRPEDQPWLL RVNGKSGRKF KGIKKGGVTE
NTSYYIFTQC PDGAFEAFPV HNWYNFTPLA RHRTLTAEEA EEEWERRNKV LNHFSIMQQR
RLKDQDQDED EEEKEKRGRR KASELRIHDL EDDLEMSSDA SDASGEEGGR VPKAKKKAPL
AKGGRKKKKK KGSDDEAFED SDDGDFEGQE VDYMSDGSSS SQEEPESKAK APQQEEGPKG
VDEQSDSSEE SEEEKPPEED KEEEEEKKAP TPQEKKRRKD SSEESDSSEE SDIDSEASSA
LFMAKKKTPP KRERKPSGGS SRGNSRPGTP SAEGGSTSST LRAAASKLEQ GKRVSEMPAA
KRLRLDTGPQ SLSGKSTPQP PSGKTTPNSG DVQVTEDAVR RYLTRKPMTT KDLLKKFQTK
KTGLSSEQTV NVLAQILKRL NPERKMINDK MHFSLKE
