ID T2FB_HUMAN Reviewed; 249 AA. AC P13984; A6NNS5; Q5W0H3; DT 01-JAN-1990, integrated into UniProtKB/Swiss-Prot. DT 01-FEB-1994, sequence version 2. DT 27-MAR-2024, entry version 223. DE RecName: Full=General transcription factor IIF subunit 2; DE AltName: Full=General transcription factor IIF 30 kDa subunit; DE AltName: Full=Transcription initiation factor IIF subunit beta; DE Short=TFIIF-beta; DE AltName: Full=Transcription initiation factor RAP30; GN Name=GTF2F2; Synonyms=RAP30; 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], PARTIAL PROTEIN SEQUENCE, AND FUNCTION. RC TISSUE=Kidney; RX PubMed=2477704; DOI=10.1038/341410a0; RA Sopta M., Burton Z.F., Greenblatt J.; RT "Structure and associated DNA-helicase activity of a general transcription RT initiation factor that binds to RNA polymerase II."; RL Nature 341:410-414(1989). RN [2] RP NUCLEOTIDE SEQUENCE [MRNA]. RX PubMed=1840667; DOI=10.1093/nar/19.19.5436; RA Horikoshi M., Fujita H., Wang J., Takada R., Roeder R.G.; RT "Nucleotide and amino acid sequence of RAP30."; RL Nucleic Acids Res. 19:5436-5436(1991). RN [3] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. RC TISSUE=Placenta; 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]. 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 (OCT-2004) to the EMBL/GenBank/DDBJ databases. RN [5] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RX PubMed=15057823; DOI=10.1038/nature02379; RA Dunham A., Matthews L.H., Burton J., Ashurst J.L., Howe K.L., RA Ashcroft K.J., Beare D.M., Burford D.C., Hunt S.E., Griffiths-Jones S., RA Jones M.C., Keenan S.J., Oliver K., Scott C.E., Ainscough R., Almeida J.P., RA Ambrose K.D., Andrews D.T., Ashwell R.I.S., Babbage A.K., Bagguley C.L., RA Bailey J., Bannerjee R., Barlow K.F., Bates K., Beasley H., Bird C.P., RA Bray-Allen S., Brown A.J., Brown J.Y., Burrill W., Carder C., Carter N.P., RA Chapman J.C., Clamp M.E., Clark S.Y., Clarke G., Clee C.M., Clegg S.C., RA Cobley V., Collins J.E., Corby N., Coville G.J., Deloukas P., Dhami P., RA Dunham I., Dunn M., Earthrowl M.E., Ellington A.G., Faulkner L., RA Frankish A.G., Frankland J., French L., Garner P., Garnett J., RA Gilbert J.G.R., Gilson C.J., Ghori J., Grafham D.V., Gribble S.M., RA Griffiths C., Hall R.E., Hammond S., Harley J.L., Hart E.A., Heath P.D., RA Howden P.J., Huckle E.J., Hunt P.J., Hunt A.R., Johnson C., Johnson D., RA Kay M., Kimberley A.M., King A., Laird G.K., Langford C.J., Lawlor S., RA Leongamornlert D.A., Lloyd D.M., Lloyd C., Loveland J.E., Lovell J., RA Martin S., Mashreghi-Mohammadi M., McLaren S.J., McMurray A., Milne S., RA Moore M.J.F., Nickerson T., Palmer S.A., Pearce A.V., Peck A.I., Pelan S., RA Phillimore B., Porter K.M., Rice C.M., Searle S., Sehra H.K., Shownkeen R., RA Skuce C.D., Smith M., Steward C.A., Sycamore N., Tester J., Thomas D.W., RA Tracey A., Tromans A., Tubby B., Wall M., Wallis J.M., West A.P., RA Whitehead S.L., Willey D.L., Wilming L., Wray P.W., Wright M.W., Young L., RA Coulson A., Durbin R.M., Hubbard T., Sulston J.E., Beck S., Bentley D.R., RA Rogers J., Ross M.T.; RT "The DNA sequence and analysis of human chromosome 13."; RL Nature 428:522-528(2004). RN [6] 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 (JUL-2005) to the EMBL/GenBank/DDBJ databases. RN [7] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. RC TISSUE=Eye; 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 [8] RP INTERACTION WITH GTF2B. RX PubMed=8504927; DOI=10.1101/gad.7.6.1021; RA Ha I., Roberts S., Maldonado E., Sun X., Kim L.U., Green M., Reinberg D.; RT "Multiple functional domains of human transcription factor IIB: distinct RT interactions with two general transcription factors and RNA polymerase RT II."; RL Genes Dev. 7:1021-1032(1993). 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 INTERACTION WITH HTATSF1, AND SUBCELLULAR LOCATION. RX PubMed=10454543; DOI=10.1128/mcb.19.9.5960; RA Kim J.B., Yamaguchi Y., Wada T., Handa H., Sharp P.A.; RT "Tat-SF1 protein associates with RAP30 and human SPT5 proteins."; RL Mol. Cell. Biol. 19:5960-5968(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 PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-142, AND IDENTIFICATION BY RP 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 [13] 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 [14] RP ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-22; LYS-33 AND LYS-137, AND RP IDENTIFICATION BY MASS 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 [15] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-248, 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 [16] 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 [17] RP STRUCTURE BY NMR OF 175-243. RX PubMed=9689043; DOI=10.1073/pnas.95.16.9117; RA Groft C.M., Uljon S.N., Wang R., Werner M.H.; RT "Structural homology between the Rap30 DNA-binding domain and linker RT histone H5: implications for preinitiation complex assembly."; RL Proc. Natl. Acad. Sci. U.S.A. 95:9117-9122(1998). RN [18] RP STRUCTURE BY ELECTRON MICROSCOPY (3.90 ANGSTROMS) IN COMPLEX WITH PROMOTER RP DNA, AND SUBUNIT. RX PubMed=27193682; DOI=10.1038/nature17970; RA He Y., Yan C., Fang J., Inouye C., Tjian R., Ivanov I., Nogales E.; RT "Near-atomic resolution visualization of human transcription promoter RT opening."; RL Nature 533:359-365(2016). 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. {ECO:0000269|PubMed:2477704}. CC -!- SUBUNIT: Heterodimer of an alpha and a beta subunit. Interacts with CC HTATSF1 and GPBP1 (By similarity). Interacts with URI1. Interacts with CC GTF2B (via N-terminus); this interaction is inhibited in presence of CC GTF2F1 (PubMed:8504927, PubMed:8662660). Part of TBP-based Pol II pre- CC initiation complex (PIC), in which Pol II core assembles with general CC transcription factors and other specific initiation factors including CC GTF2E1, GTF2E2, GTF2F1, GTF2F2, TCEA1, ERCC2, ERCC3, GTF2H2, GTF2H3, CC GTF2H4, GTF2H5, GTF2A1, GTF2A2, GTF2B and TBP; this large multi-subunit CC PIC complex mediates DNA unwinding and targets Pol II core to the CC transcription start site where the first phosphodiester bond forms. CC {ECO:0000250, ECO:0000269|PubMed:10454543, ECO:0000269|PubMed:12737519, CC ECO:0000269|PubMed:27193682, ECO:0000269|PubMed:8504927, CC ECO:0000269|PubMed:8662660}. CC -!- INTERACTION: CC P13984; Q8WW35: DYNLT2B; NbExp=2; IntAct=EBI-1030560, EBI-2692044; CC P13984; Q14192: FHL2; NbExp=3; IntAct=EBI-1030560, EBI-701903; CC P13984; P35269: GTF2F1; NbExp=16; IntAct=EBI-1030560, EBI-457886; CC P13984; Q9UPY8: MAPRE3; NbExp=3; IntAct=EBI-1030560, EBI-726739; CC P13984; P46776: RPL27A; NbExp=2; IntAct=EBI-1030560, EBI-350581; CC P13984; O94763: URI1; NbExp=4; IntAct=EBI-1030560, EBI-357067; CC P13984; Q96E35: ZMYND19; NbExp=3; IntAct=EBI-1030560, EBI-746595; CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:10454543}. CC -!- SIMILARITY: Belongs to the TFIIF beta subunit family. {ECO:0000305}. CC -!- CAUTION: GTF2F2 appears to have ATP-dependent DNA-helicase activity; CC however this is probably an artifact that happened during the protein CC purification. {ECO:0000305|PubMed:2477704}. 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; X16901; CAA34775.1; -; mRNA. DR EMBL; X59745; CAA42419.1; -; mRNA. DR EMBL; AK291545; BAF84234.1; -; mRNA. DR EMBL; BT019525; AAV38332.1; -; mRNA. DR EMBL; AL138963; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; AL138693; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; CH471075; EAX08728.1; -; Genomic_DNA. DR EMBL; BC001771; AAH01771.1; -; mRNA. DR CCDS; CCDS9395.1; -. DR PIR; S06141; S06141. DR PIR; S18677; S18677. DR RefSeq; NP_004119.1; NM_004128.2. DR PDB; 1BBY; NMR; -; A=175-243. DR PDB; 1F3U; X-ray; 1.70 A; A/C/E/G=2-119. DR PDB; 2BBY; NMR; -; A=175-243. DR PDB; 5IY6; EM; 7.20 A; T=1-249. DR PDB; 5IY7; EM; 8.60 A; T=1-249. DR PDB; 5IY8; EM; 7.90 A; T=1-249. DR PDB; 5IY9; EM; 6.30 A; T=1-249. DR PDB; 5IYA; EM; 5.40 A; T=1-249. DR PDB; 5IYB; EM; 3.90 A; T=1-249. DR PDB; 5IYC; EM; 3.90 A; T=1-249. DR PDB; 5IYD; EM; 3.90 A; T=1-249. DR PDB; 6O9L; EM; 7.20 A; T=1-249. DR PDB; 7EDX; EM; 4.50 A; T=1-249. DR PDB; 7EG7; EM; 6.20 A; T=1-249. DR PDB; 7EG8; EM; 7.40 A; T=1-249. DR PDB; 7EG9; EM; 3.70 A; T=1-249. DR PDB; 7EGA; EM; 4.10 A; T=1-249. DR PDB; 7EGB; EM; 3.30 A; T=1-249. DR PDB; 7EGC; EM; 3.90 A; T=1-249. DR PDB; 7ENA; EM; 4.07 A; FB=1-249. DR PDB; 7ENC; EM; 4.13 A; FB=1-249. DR PDB; 7LBM; EM; 4.80 A; T=1-249. DR PDB; 7NVR; EM; 4.50 A; R=1-249. DR PDB; 7NVS; EM; 2.80 A; R=1-249. DR PDB; 7NVT; EM; 2.90 A; R=1-249. DR PDB; 7NVU; EM; 2.50 A; R=1-249. DR PDB; 7NVY; EM; 7.30 A; R=1-249. DR PDB; 7NVZ; EM; 7.20 A; R=1-249. DR PDB; 7NW0; EM; 6.60 A; R=1-249. DR PDB; 7ZWD; EM; 3.00 A; R=1-249. DR PDB; 7ZX7; EM; 3.40 A; R=1-249. DR PDB; 7ZX8; EM; 3.00 A; R=1-249. DR PDB; 8BVW; EM; 4.00 A; R=1-249. DR PDB; 8BYQ; EM; 4.10 A; R=1-249. DR PDB; 8BZ1; EM; 3.80 A; R=1-249. DR PDB; 8GXQ; EM; 5.04 A; FB=1-249. DR PDB; 8GXS; EM; 4.16 A; FB=1-249. DR PDB; 8WAK; EM; 5.47 A; T=1-249. DR PDB; 8WAL; EM; 8.52 A; T=1-249. DR PDB; 8WAN; EM; 6.07 A; T=1-249. DR PDB; 8WAO; EM; 6.40 A; T=1-249. DR PDB; 8WAP; EM; 5.85 A; T=1-249. DR PDB; 8WAQ; EM; 6.29 A; T=1-249. DR PDB; 8WAR; EM; 7.20 A; T=1-249. DR PDB; 8WAS; EM; 6.13 A; T=1-249. DR PDB; 8WAT; EM; 2.82 A; T=1-249. DR PDB; 8WAU; EM; 2.78 A; T=1-249. DR PDB; 8WAV; EM; 2.72 A; T=1-249. DR PDB; 8WAW; EM; 3.02 A; T=1-249. DR PDB; 8WAX; EM; 2.75 A; T=1-249. DR PDB; 8WAY; EM; 2.85 A; T=1-249. DR PDB; 8WAZ; EM; 2.76 A; T=1-249. DR PDB; 8WB0; EM; 2.94 A; T=1-249. DR PDBsum; 1BBY; -. DR PDBsum; 1F3U; -. DR PDBsum; 2BBY; -. 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 PDBsum; 7ZWD; -. DR PDBsum; 7ZX7; -. DR PDBsum; 7ZX8; -. DR PDBsum; 8BVW; -. DR PDBsum; 8BYQ; -. DR PDBsum; 8BZ1; -. 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 PDBsum; 8WAT; -. DR PDBsum; 8WAU; -. DR PDBsum; 8WAV; -. DR PDBsum; 8WAW; -. DR PDBsum; 8WAX; -. DR PDBsum; 8WAY; -. DR PDBsum; 8WAZ; -. DR PDBsum; 8WB0; -. DR AlphaFoldDB; P13984; -. DR EMDB; EMD-12610; -. DR EMDB; EMD-12611; -. DR EMDB; EMD-12612; -. DR EMDB; EMD-12613; -. DR EMDB; EMD-12617; -. DR EMDB; EMD-12618; -. DR EMDB; EMD-12619; -. DR EMDB; EMD-14997; -. DR EMDB; EMD-15006; -. DR EMDB; EMD-15007; -. DR EMDB; EMD-16274; -. DR EMDB; EMD-16331; -. DR EMDB; EMD-16335; -. DR EMDB; EMD-23255; -. DR EMDB; EMD-31075; -. DR EMDB; EMD-31107; -. DR EMDB; EMD-31108; -. DR EMDB; EMD-31109; -. DR EMDB; EMD-31110; -. DR EMDB; EMD-31111; -. DR EMDB; EMD-31112; -. DR EMDB; EMD-31204; -. DR EMDB; EMD-31207; -. DR EMDB; EMD-34359; -. DR EMDB; EMD-34360; -. DR EMDB; EMD-8132; -. DR EMDB; EMD-8133; -. DR EMDB; EMD-8134; -. DR EMDB; EMD-8135; -. DR EMDB; EMD-8136; -. DR EMDB; EMD-8137; -. DR EMDB; EMD-8138; -. DR SMR; P13984; -. DR BioGRID; 109218; 131. DR ComplexPortal; CPX-79; General transcription factor TFIIF complex. DR CORUM; P13984; -. DR DIP; DIP-41680N; -. DR IntAct; P13984; 56. DR MINT; P13984; -. DR STRING; 9606.ENSP00000340823; -. DR GlyGen; P13984; 1 site, 1 O-linked glycan (1 site). DR iPTMnet; P13984; -. DR PhosphoSitePlus; P13984; -. DR BioMuta; GTF2F2; -. DR DMDM; 464519; -. DR EPD; P13984; -. DR jPOST; P13984; -. DR MassIVE; P13984; -. DR MaxQB; P13984; -. DR PaxDb; 9606-ENSP00000340823; -. DR PeptideAtlas; P13984; -. DR ProteomicsDB; 53012; -. DR Pumba; P13984; -. DR Antibodypedia; 1838; 314 antibodies from 30 providers. DR DNASU; 2963; -. DR Ensembl; ENST00000340473.8; ENSP00000340823.6; ENSG00000188342.13. DR GeneID; 2963; -. DR KEGG; hsa:2963; -. DR MANE-Select; ENST00000340473.8; ENSP00000340823.6; NM_004128.3; NP_004119.1. DR UCSC; uc001uzw.4; human. DR AGR; HGNC:4653; -. DR CTD; 2963; -. DR DisGeNET; 2963; -. DR GeneCards; GTF2F2; -. DR HGNC; HGNC:4653; GTF2F2. DR HPA; ENSG00000188342; Low tissue specificity. DR MIM; 189969; gene. DR neXtProt; NX_P13984; -. DR OpenTargets; ENSG00000188342; -. DR PharmGKB; PA29039; -. DR VEuPathDB; HostDB:ENSG00000188342; -. DR eggNOG; KOG2905; Eukaryota. DR GeneTree; ENSGT00390000016051; -. DR HOGENOM; CLU_047858_1_0_1; -. DR InParanoid; P13984; -. DR OMA; NKWEKAP; -. DR OrthoDB; 4916937at2759; -. DR PhylomeDB; P13984; -. DR TreeFam; TF314290; -. DR PathwayCommons; P13984; -. 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; P13984; -. DR SIGNOR; P13984; -. DR BioGRID-ORCS; 2963; 643 hits in 1158 CRISPR screens. DR ChiTaRS; GTF2F2; human. DR EvolutionaryTrace; P13984; -. DR GeneWiki; GTF2F2; -. DR GenomeRNAi; 2963; -. DR Pharos; P13984; Tbio. DR PRO; PR:P13984; -. DR Proteomes; UP000005640; Chromosome 13. DR RNAct; P13984; Protein. DR Bgee; ENSG00000188342; Expressed in primordial germ cell in gonad and 199 other cell types or tissues. DR ExpressionAtlas; P13984; baseline and differential. DR GO; GO:0015630; C:microtubule cytoskeleton; IDA:HPA. DR GO; GO:0005654; C:nucleoplasm; IDA:HPA. DR GO; GO:0005634; C:nucleus; IDA:CAFA. DR GO; GO:0005674; C:transcription factor TFIIF complex; IPI:ComplexPortal. DR GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW. DR GO; GO:0016251; F:RNA polymerase II general transcription initiation factor activity; ISS:ARUK-UCL. DR GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; IDA:ComplexPortal. DR GO; GO:0006366; P:transcription by RNA polymerase II; IMP:UniProtKB. DR GO; GO:0006368; P:transcription elongation by RNA polymerase II; IDA:ComplexPortal. DR GO; GO:0006367; P:transcription initiation at RNA polymerase II promoter; IDA:ComplexPortal. DR CDD; cd07980; TFIIF_beta; 1. DR Gene3D; 1.10.10.10; Winged helix-like DNA-binding domain superfamily/Winged helix DNA-binding domain; 1. DR InterPro; IPR003196; TFIIF_beta. DR InterPro; IPR040450; TFIIF_beta_HTH. DR InterPro; IPR040504; TFIIF_beta_N. DR InterPro; IPR011039; TFIIF_interaction. DR InterPro; IPR036388; WH-like_DNA-bd_sf. DR InterPro; IPR036390; WH_DNA-bd_sf. DR PANTHER; PTHR10445; GENERAL TRANSCRIPTION FACTOR IIF SUBUNIT 2; 1. DR PANTHER; PTHR10445:SF0; GENERAL TRANSCRIPTION FACTOR IIF SUBUNIT 2; 1. DR Pfam; PF02270; TFIIF_beta; 1. DR Pfam; PF17683; TFIIF_beta_N; 1. DR PIRSF; PIRSF015849; TFIIF-beta; 1. DR SUPFAM; SSF50916; Rap30/74 interaction domains; 1. DR SUPFAM; SSF46785; Winged helix' DNA-binding domain; 1. DR Genevisible; P13984; HS. 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 CHAIN 2..249 FT /note="General transcription factor IIF subunit 2" FT /id="PRO_0000211235" FT BINDING 227 FT /ligand="DNA" FT /ligand_id="ChEBI:CHEBI:16991" FT /evidence="ECO:0000269|PubMed:27193682, FT ECO:0007744|PDB:5IYD" FT BINDING 229 FT /ligand="DNA" FT /ligand_id="ChEBI:CHEBI:16991" FT /evidence="ECO:0000269|PubMed:27193682, FT ECO:0007744|PDB:5IYD" FT MOD_RES 2 FT /note="N-acetylalanine" FT /evidence="ECO:0007744|PubMed:19413330" FT MOD_RES 22 FT /note="N6-acetyllysine" FT /evidence="ECO:0007744|PubMed:19608861" FT MOD_RES 33 FT /note="N6-acetyllysine" FT /evidence="ECO:0007744|PubMed:19608861" FT MOD_RES 137 FT /note="N6-acetyllysine" FT /evidence="ECO:0007744|PubMed:19608861" FT MOD_RES 142 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:18669648" FT MOD_RES 248 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:20068231" FT STRAND 6..8 FT /evidence="ECO:0007829|PDB:1F3U" FT HELIX 10..13 FT /evidence="ECO:0007829|PDB:1F3U" FT STRAND 17..24 FT /evidence="ECO:0007829|PDB:1F3U" FT HELIX 25..31 FT /evidence="ECO:0007829|PDB:1F3U" FT STRAND 39..48 FT /evidence="ECO:0007829|PDB:1F3U" FT STRAND 51..58 FT /evidence="ECO:0007829|PDB:1F3U" FT HELIX 60..63 FT /evidence="ECO:0007829|PDB:1F3U" FT STRAND 80..86 FT /evidence="ECO:0007829|PDB:1F3U" FT STRAND 91..99 FT /evidence="ECO:0007829|PDB:1F3U" FT STRAND 104..116 FT /evidence="ECO:0007829|PDB:1F3U" FT HELIX 123..136 FT /evidence="ECO:0007829|PDB:7NVU" FT STRAND 143..147 FT /evidence="ECO:0007829|PDB:7NVU" FT HELIX 160..172 FT /evidence="ECO:0007829|PDB:7NVU" FT HELIX 180..193 FT /evidence="ECO:0007829|PDB:7NVU" FT STRAND 195..197 FT /evidence="ECO:0007829|PDB:7NVU" FT HELIX 199..206 FT /evidence="ECO:0007829|PDB:7NVU" FT HELIX 210..220 FT /evidence="ECO:0007829|PDB:7NVU" FT STRAND 222..224 FT /evidence="ECO:0007829|PDB:7NVU" FT STRAND 227..229 FT /evidence="ECO:0007829|PDB:7NVU" FT STRAND 232..234 FT /evidence="ECO:0007829|PDB:7NVU" SQ SEQUENCE 249 AA; 28380 MW; 05A1A9F8D31B749C CRC64; MAERGELDLT GAKQNTGVWL VKVPKYLSQQ WAKASGRGEV GKLRIAKTQG RTEVSFTLNE DLANIHDIGG KPASVSAPRE HPFVLQSVGG QTLTVFTESS SDKLSLEGIV VQRAECRPAA SENYMRLKRL QIEESSKPVR LSQQLDKVVT TNYKPVANHQ YNIEYERKKK EDGKRARADK QHVLDMLFSA FEKHQYYNLK DLVDITKQPV VYLKEILKEI GVQNVKGIHK NTWELKPEYR HYQGEEKSD //