T2FB_HUMAN
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 03-AUG-2022, entry version 214.
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).
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). {ECO:0000250,
CC ECO:0000269|PubMed:10454543, ECO:0000269|PubMed:12737519,
CC ECO:0000269|PubMed:8504927, 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}.
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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 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 AlphaFoldDB; P13984; -.
DR SMR; P13984; -.
DR BioGRID; 109218; 110.
DR ComplexPortal; CPX-79; Transcription factor TFIIF complex.
DR CORUM; P13984; -.
DR DIP; DIP-41680N; -.
DR IntAct; P13984; 54.
DR MINT; P13984; -.
DR STRING; 9606.ENSP00000340823; -.
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; P13984; -.
DR PeptideAtlas; P13984; -.
DR PRIDE; P13984; -.
DR ProteomicsDB; 53012; -.
DR Antibodypedia; 1838; 281 antibodies from 30 providers.
DR DNASU; 2963; -.
DR Ensembl; ENST00000340473.8; ENSP00000340823.6; ENSG00000188342.12.
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 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; KYIANKW; -.
DR OrthoDB; 1496393at2759; -.
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; 617 hits in 1080 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 ventricular zone and 197 other tissues.
DR ExpressionAtlas; P13984; baseline and differential.
DR Genevisible; P13984; HS.
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:0097550; C:transcription preinitiation complex; IDA:CAFA.
DR GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
DR GO; GO:0003678; F:DNA helicase activity; IEA:UniProtKB-EC.
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 from RNA polymerase II promoter; IDA:ComplexPortal.
DR GO; GO:0006367; P:transcription initiation from RNA polymerase II promoter; IDA:ComplexPortal.
DR Gene3D; 1.10.10.10; -; 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; PTHR10445; 1.
DR Pfam; PF02270; TFIIF_beta; 1.
DR Pfam; PF17683; TFIIF_beta_N; 1.
DR PIRSF; PIRSF015849; TFIIF-beta; 1.
DR SUPFAM; SSF46785; SSF46785; 1.
DR SUPFAM; SSF50916; SSF50916; 1.
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 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
