ID TF3B_HUMAN Reviewed; 677 AA. AC Q92994; B3KU36; B4DIG5; B7Z2N3; F5H5Z7; F8WA46; Q13223; Q3SYD9; Q5PR24; AC Q6IQ02; Q96KX3; Q9HCW6; Q9HCW7; Q9HCW8; DT 02-MAY-2002, integrated into UniProtKB/Swiss-Prot. DT 01-FEB-1997, sequence version 1. DT 24-JAN-2024, entry version 195. DE RecName: Full=Transcription factor IIIB 90 kDa subunit; DE Short=TFIIIB90; DE Short=hTFIIIB90; DE AltName: Full=B-related factor 1; DE Short=BRF-1; DE Short=hBRF; DE AltName: Full=TAF3B2; DE AltName: Full=TATA box-binding protein-associated factor, RNA polymerase III, subunit 2; GN Name=BRF1; Synonyms=BRF, GTF3B, TAF3B2, TAF3C; 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] (ISOFORM 1), AND PROTEIN SEQUENCE OF 264-281; RP 314-338; 441-469 AND 471-488. RX PubMed=7624363; DOI=10.1073/pnas.92.15.7026; RA Wang Z., Roeder R.G.; RT "Structure and function of a human transcription factor TFIIIB subunit that RT is evolutionarily conserved and contains both TFIIB- and high-mobility- RT group protein 2-related domains."; RL Proc. Natl. Acad. Sci. U.S.A. 92:7026-7030(1995). RN [2] RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), AND PROTEIN SEQUENCE OF 248-254; RP 263-280; 313-320; 343-348; 380-396; 440-449; 471-488; 514-527; 538-561 AND RP 570-602. RX PubMed=8943358; DOI=10.1128/mcb.16.12.7031; RA Mital R., Kobayashi R., Hernandez N.; RT "RNA polymerase III transcription from the human U6 and adenovirus type 2 RT VAI promoters has different requirements for human BRF, a subunit of human RT TFIIIB."; RL Mol. Cell. Biol. 16:7031-7042(1996). RN [3] RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 2; 3 AND 4). RX PubMed=10921893; DOI=10.1093/emboj/19.15.4134; RA McCulloch V., Hardin P., Peng W., Ruppert J.M., Lobo-Ruppert S.M.; RT "Alternatively spliced hBRF variants function at different RNA polymerase RT III promoters."; RL EMBO J. 19:4134-4143(2000). RN [4] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 7; 8 AND 9). RC TISSUE=Brain, and Hippocampus; 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]. RX PubMed=12508121; DOI=10.1038/nature01348; RA Heilig R., Eckenberg R., Petit J.-L., Fonknechten N., Da Silva C., RA Cattolico L., Levy M., Barbe V., De Berardinis V., Ureta-Vidal A., RA Pelletier E., Vico V., Anthouard V., Rowen L., Madan A., Qin S., Sun H., RA Du H., Pepin K., Artiguenave F., Robert C., Cruaud C., Bruels T., RA Jaillon O., Friedlander L., Samson G., Brottier P., Cure S., Segurens B., RA Aniere F., Samain S., Crespeau H., Abbasi N., Aiach N., Boscus D., RA Dickhoff R., Dors M., Dubois I., Friedman C., Gouyvenoux M., James R., RA Madan A., Mairey-Estrada B., Mangenot S., Martins N., Menard M., Oztas S., RA Ratcliffe A., Shaffer T., Trask B., Vacherie B., Bellemere C., Belser C., RA Besnard-Gonnet M., Bartol-Mavel D., Boutard M., Briez-Silla S., RA Combette S., Dufosse-Laurent V., Ferron C., Lechaplais C., Louesse C., RA Muselet D., Magdelenat G., Pateau E., Petit E., Sirvain-Trukniewicz P., RA Trybou A., Vega-Czarny N., Bataille E., Bluet E., Bordelais I., Dubois M., RA Dumont C., Guerin T., Haffray S., Hammadi R., Muanga J., Pellouin V., RA Robert D., Wunderle E., Gauguet G., Roy A., Sainte-Marthe L., Verdier J., RA Verdier-Discala C., Hillier L.W., Fulton L., McPherson J., Matsuda F., RA Wilson R., Scarpelli C., Gyapay G., Wincker P., Saurin W., Quetier F., RA Waterston R., Hood L., Weissenbach J.; RT "The DNA sequence and analysis of human chromosome 14."; RL Nature 421:601-607(2003). 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] (ISOFORMS 2; 5 AND 6). RC TISSUE=Brain, Skin, and Testis; 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 BDP1. RX PubMed=14592981; DOI=10.1093/emboj/cdg544; RA Fairley J.A., Scott P.H., White R.J.; RT "TFIIIB is phosphorylated, disrupted and selectively released from tRNA RT promoters during mitosis in vivo."; RL EMBO J. 22:5841-5850(2003). RN [9] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-553, 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 [10] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-365 AND SER-450, 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 [11] RP INTERACTION WITH MAF1. RX PubMed=18377933; DOI=10.1016/j.jmb.2008.02.060; RA Goodfellow S.J., Graham E.L., Kantidakis T., Marshall L., Coppins B.A., RA Oficjalska-Pham D., Gerard M., Lefebvre O., White R.J.; RT "Regulation of RNA polymerase III transcription by Maf1 in mammalian RT cells."; RL J. Mol. Biol. 378:481-491(2008). RN [12] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-365, 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 [13] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-553, AND IDENTIFICATION BY RP MASS 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 [14] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-553, AND IDENTIFICATION BY RP 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 [15] RP INVOLVEMENT IN CFDS, AND VARIANTS CFDS TRP-223; LEU-226; MET-259 AND RP HIS-292. RX PubMed=25561519; DOI=10.1101/gr.176925.114; RA Borck G., Hog F., Dentici M.L., Tan P.L., Sowada N., Medeira A., RA Gueneau L., Thiele H., Kousi M., Lepri F., Wenzeck L., Blumenthal I., RA Radicioni A., Schwarzenberg T.L., Mandriani B., Fischetto R., RA Morris-Rosendahl D.J., Altmuller J., Reymond A., Nurnberg P., Merla G., RA Dallapiccola B., Katsanis N., Cramer P., Kubisch C.; RT "BRF1 mutations alter RNA polymerase III-dependent transcription and cause RT neurodevelopmental anomalies."; RL Genome Res. 25:155-166(2015). RN [16] RP VARIANT [LARGE SCALE ANALYSIS] MET-542. RX PubMed=16959974; DOI=10.1126/science.1133427; RA Sjoeblom T., Jones S., Wood L.D., Parsons D.W., Lin J., Barber T.D., RA Mandelker D., Leary R.J., Ptak J., Silliman N., Szabo S., Buckhaults P., RA Farrell C., Meeh P., Markowitz S.D., Willis J., Dawson D., Willson J.K.V., RA Gazdar A.F., Hartigan J., Wu L., Liu C., Parmigiani G., Park B.H., RA Bachman K.E., Papadopoulos N., Vogelstein B., Kinzler K.W., RA Velculescu V.E.; RT "The consensus coding sequences of human breast and colorectal cancers."; RL Science 314:268-274(2006). CC -!- FUNCTION: General activator of RNA polymerase which utilizes different CC TFIIIB complexes at structurally distinct promoters. The isoform 1 is CC involved in the transcription of tRNA, adenovirus VA1, 7SL and 5S RNA. CC Isoform 2 is required for transcription of the U6 promoter. CC -!- SUBUNIT: TFIIIB comprises at least the TATA-binding protein (TBP) and CC the B-related factor 1 (BRF1/TFIIIB90). Interacts with BDP1 CC (PubMed:14592981). Interacts with MAF1 (PubMed:18377933). CC {ECO:0000269|PubMed:14592981, ECO:0000269|PubMed:18377933}. CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250}. CC -!- ALTERNATIVE PRODUCTS: CC Event=Alternative splicing; Named isoforms=9; CC Name=1; Synonyms=hBRF1; CC IsoId=Q92994-1; Sequence=Displayed; CC Name=2; Synonyms=hBRF2; CC IsoId=Q92994-2; Sequence=VSP_006396, VSP_006397, VSP_006398; CC Name=3; Synonyms=hBRF3; CC IsoId=Q92994-3; Sequence=VSP_006396; CC Name=4; Synonyms=hBRF4; CC IsoId=Q92994-4; Sequence=VSP_006399, VSP_006400; CC Name=5; CC IsoId=Q92994-5; Sequence=VSP_014697; CC Name=6; CC IsoId=Q92994-6; Sequence=VSP_043835, VSP_043836; CC Name=7; CC IsoId=Q92994-7; Sequence=VSP_044244; CC Name=8; CC IsoId=Q92994-8; Sequence=VSP_044244, VSP_045046; CC Name=9; CC IsoId=Q92994-9; Sequence=VSP_045045; CC -!- DISEASE: Cerebellofaciodental syndrome (CFDS) [MIM:616202]: An CC autosomal recessive disorder characterized by cerebellar hypoplasia, CC delayed development and intellectual disability, as well as facial CC dysmorphic features, short stature, microcephaly, and dental anomalies. CC {ECO:0000269|PubMed:25561519}. Note=The disease is caused by variants CC affecting the gene represented in this entry. CC -!- SIMILARITY: Belongs to the TFIIB family. {ECO:0000305}. CC -!- SEQUENCE CAUTION: CC Sequence=AAC50170.1; Type=Frameshift; Evidence={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; U28838; AAC50170.1; ALT_FRAME; mRNA. DR EMBL; U75276; AAB38876.1; -; mRNA. DR EMBL; AJ297406; CAC04512.1; -; mRNA. DR EMBL; AJ297407; CAC04513.1; -; mRNA. DR EMBL; AJ297408; CAC04514.1; -; mRNA. DR EMBL; AK096471; BAG53298.1; -; mRNA. DR EMBL; AK294899; BAH11919.1; -; mRNA. DR EMBL; AK295579; BAG58477.1; -; mRNA. DR EMBL; AL512355; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; CH471061; EAW81908.1; -; Genomic_DNA. DR EMBL; CH471061; EAW81911.1; -; Genomic_DNA. DR EMBL; BC016743; AAH16743.1; -; mRNA. DR EMBL; BC071637; AAH71637.1; -; mRNA. DR EMBL; BC086856; AAH86856.1; -; mRNA. DR EMBL; BC103859; AAI03860.1; -; mRNA. DR CCDS; CCDS10001.1; -. [Q92994-1] DR CCDS; CCDS42001.1; -. [Q92994-3] DR CCDS; CCDS55949.1; -. [Q92994-9] DR CCDS; CCDS55950.1; -. [Q92994-7] DR CCDS; CCDS55951.1; -. [Q92994-8] DR CCDS; CCDS55952.1; -. [Q92994-5] DR CCDS; CCDS55953.1; -. [Q92994-6] DR PIR; I39065; I39065. DR RefSeq; NP_001229715.1; NM_001242786.1. [Q92994-8] DR RefSeq; NP_001229716.1; NM_001242787.1. [Q92994-7] DR RefSeq; NP_001229717.1; NM_001242788.1. [Q92994-5] DR RefSeq; NP_001229718.1; NM_001242789.1. [Q92994-9] DR RefSeq; NP_001229719.1; NM_001242790.1. [Q92994-6] DR RefSeq; NP_001510.2; NM_001519.3. [Q92994-1] DR RefSeq; NP_663718.1; NM_145685.2. [Q92994-3] DR RefSeq; XP_005267620.1; XM_005267563.3. [Q92994-3] DR AlphaFoldDB; Q92994; -. DR SMR; Q92994; -. DR BioGRID; 109227; 98. DR ComplexPortal; CPX-2396; General transcription factor TFIII3B complex, BRF1 variant. DR CORUM; Q92994; -. DR IntAct; Q92994; 12. DR MINT; Q92994; -. DR STRING; 9606.ENSP00000448387; -. DR ChEMBL; CHEMBL4523421; -. DR GlyGen; Q92994; 1 site, 1 O-linked glycan (1 site). DR iPTMnet; Q92994; -. DR PhosphoSitePlus; Q92994; -. DR BioMuta; BRF1; -. DR DMDM; 20455319; -. DR EPD; Q92994; -. DR jPOST; Q92994; -. DR MassIVE; Q92994; -. DR MaxQB; Q92994; -. DR PaxDb; 9606-ENSP00000448323; -. DR PeptideAtlas; Q92994; -. DR ProteomicsDB; 27032; -. DR ProteomicsDB; 30432; -. DR ProteomicsDB; 75658; -. [Q92994-1] DR ProteomicsDB; 75659; -. [Q92994-2] DR ProteomicsDB; 75660; -. [Q92994-3] DR ProteomicsDB; 75661; -. [Q92994-4] DR ProteomicsDB; 75662; -. [Q92994-5] DR ProteomicsDB; 75663; -. [Q92994-6] DR Pumba; Q92994; -. DR Antibodypedia; 14980; 292 antibodies from 29 providers. DR DNASU; 2972; -. DR Ensembl; ENST00000327359.7; ENSP00000329029.3; ENSG00000185024.18. [Q92994-7] DR Ensembl; ENST00000379937.6; ENSP00000369269.2; ENSG00000185024.18. [Q92994-5] DR Ensembl; ENST00000392557.8; ENSP00000376340.4; ENSG00000185024.18. [Q92994-3] DR Ensembl; ENST00000440513.7; ENSP00000388877.3; ENSG00000185024.18. [Q92994-8] DR Ensembl; ENST00000446501.6; ENSP00000389859.2; ENSG00000185024.18. [Q92994-9] DR Ensembl; ENST00000547530.7; ENSP00000448387.2; ENSG00000185024.18. [Q92994-1] DR Ensembl; ENST00000548421.2; ENSP00000446707.1; ENSG00000185024.18. [Q92994-6] DR GeneID; 2972; -. DR KEGG; hsa:2972; -. DR MANE-Select; ENST00000547530.7; ENSP00000448387.2; NM_001519.4; NP_001510.2. DR UCSC; uc001yql.3; human. [Q92994-1] DR AGR; HGNC:11551; -. DR CTD; 2972; -. DR DisGeNET; 2972; -. DR GeneCards; BRF1; -. DR HGNC; HGNC:11551; BRF1. DR HPA; ENSG00000185024; Low tissue specificity. DR MalaCards; BRF1; -. DR MIM; 604902; gene. DR MIM; 616202; phenotype. DR neXtProt; NX_Q92994; -. DR OpenTargets; ENSG00000185024; -. DR Orphanet; 444072; Cerebellar-facial-dental syndrome. DR PharmGKB; PA164741296; -. DR VEuPathDB; HostDB:ENSG00000185024; -. DR eggNOG; KOG1598; Eukaryota. DR GeneTree; ENSGT00390000010349; -. DR HOGENOM; CLU_010293_2_3_1; -. DR InParanoid; Q92994; -. DR OMA; AEPPCKV; -. DR OrthoDB; 5483352at2759; -. DR PhylomeDB; Q92994; -. DR TreeFam; TF324046; -. DR PathwayCommons; Q92994; -. DR Reactome; R-HSA-749476; RNA Polymerase III Abortive And Retractive Initiation. DR Reactome; R-HSA-76061; RNA Polymerase III Transcription Initiation From Type 1 Promoter. DR Reactome; R-HSA-76066; RNA Polymerase III Transcription Initiation From Type 2 Promoter. DR SignaLink; Q92994; -. DR SIGNOR; Q92994; -. DR BioGRID-ORCS; 2972; 799 hits in 1161 CRISPR screens. DR ChiTaRS; BRF1; human. DR GeneWiki; BRF1_(gene); -. DR GenomeRNAi; 2972; -. DR Pharos; Q92994; Tbio. DR PRO; PR:Q92994; -. DR Proteomes; UP000005640; Chromosome 14. DR RNAct; Q92994; Protein. DR Bgee; ENSG00000185024; Expressed in sural nerve and 129 other cell types or tissues. DR ExpressionAtlas; Q92994; baseline and differential. DR GO; GO:0005654; C:nucleoplasm; TAS:Reactome. DR GO; GO:0005634; C:nucleus; IBA:GO_Central. DR GO; GO:0000126; C:transcription factor TFIIIB complex; IBA:GO_Central. DR GO; GO:0097550; C:transcription preinitiation complex; IBA:GO_Central. DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW. DR GO; GO:0000995; F:RNA polymerase III general transcription initiation factor activity; IBA:GO_Central. DR GO; GO:0001006; F:RNA polymerase III type 3 promoter sequence-specific DNA binding; IBA:GO_Central. DR GO; GO:0017025; F:TBP-class protein binding; IEA:InterPro. DR GO; GO:0006352; P:DNA-templated transcription initiation; IBA:GO_Central. DR GO; GO:0045945; P:positive regulation of transcription by RNA polymerase III; IEA:Ensembl. DR GO; GO:0009303; P:rRNA transcription; TAS:ProtInc. DR GO; GO:0006383; P:transcription by RNA polymerase III; IBA:GO_Central. DR GO; GO:0006384; P:transcription initiation at RNA polymerase III promoter; TAS:ProtInc. DR GO; GO:0070897; P:transcription preinitiation complex assembly; IEA:InterPro. DR GO; GO:0009304; P:tRNA transcription; TAS:ProtInc. DR CDD; cd20553; CYCLIN_TFIIIB90_rpt1; 1. DR CDD; cd20554; CYCLIN_TFIIIB90_rpt2; 1. DR Gene3D; 2.20.25.10; -; 1. DR Gene3D; 1.10.472.10; Cyclin-like; 2. DR Gene3D; 1.20.5.650; Single helix bin; 1. DR InterPro; IPR011665; BRF1_TBP-bd_dom. DR InterPro; IPR013763; Cyclin-like_dom. DR InterPro; IPR036915; Cyclin-like_sf. DR InterPro; IPR000812; TFIIB. DR InterPro; IPR013150; TFIIB_cyclin. DR InterPro; IPR013137; Znf_TFIIB. DR PANTHER; PTHR11618:SF4; TRANSCRIPTION FACTOR IIIB 90 KDA SUBUNIT; 1. DR PANTHER; PTHR11618; TRANSCRIPTION INITIATION FACTOR IIB-RELATED; 1. DR Pfam; PF07741; BRF1; 1. DR Pfam; PF08271; TF_Zn_Ribbon; 1. DR Pfam; PF00382; TFIIB; 2. DR PRINTS; PR00685; TIFACTORIIB. DR SMART; SM00385; CYCLIN; 2. DR SUPFAM; SSF47954; Cyclin-like; 2. DR SUPFAM; SSF57783; Zinc beta-ribbon; 1. DR PROSITE; PS51134; ZF_TFIIB; 1. DR Genevisible; Q92994; HS. PE 1: Evidence at protein level; KW Activator; Alternative splicing; Direct protein sequencing; KW Disease variant; Dwarfism; Intellectual disability; Metal-binding; Nucleus; KW Phosphoprotein; Reference proteome; Repeat; Transcription; KW Transcription regulation; Zinc; Zinc-finger. FT CHAIN 1..677 FT /note="Transcription factor IIIB 90 kDa subunit" FT /id="PRO_0000119347" FT REPEAT 91..172 FT /note="1" FT REPEAT 185..269 FT /note="2" FT ZN_FING 2..33 FT /note="TFIIB-type" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00469" FT REGION 340..368 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 385..413 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 501..521 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 544..653 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 639..653 FT /note="Acidic residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT BINDING 6 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00469" FT BINDING 9 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00469" FT BINDING 25 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00469" FT BINDING 28 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00469" FT MOD_RES 365 FT /note="Phosphothreonine" FT /evidence="ECO:0007744|PubMed:18669648, FT ECO:0007744|PubMed:19690332" FT MOD_RES 450 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:18669648" FT MOD_RES 553 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:17081983, FT ECO:0007744|PubMed:23186163, ECO:0007744|PubMed:24275569" FT VAR_SEQ 1..238 FT /note="Missing (in isoform 9)" FT /evidence="ECO:0000303|PubMed:14702039" FT /id="VSP_045045" FT VAR_SEQ 1..204 FT /note="Missing (in isoform 2 and isoform 3)" FT /evidence="ECO:0000303|PubMed:10921893, FT ECO:0000303|PubMed:15489334" FT /id="VSP_006396" FT VAR_SEQ 1..115 FT /note="Missing (in isoform 7 and isoform 8)" FT /evidence="ECO:0000303|PubMed:14702039" FT /id="VSP_044244" FT VAR_SEQ 63..89 FT /note="Missing (in isoform 5)" FT /evidence="ECO:0000303|PubMed:15489334" FT /id="VSP_014697" FT VAR_SEQ 159..242 FT /note="NVYVLGKTFLLLARELCINAPAIDPCLYIPRFAHLLEFGEKNHEVSMTALRL FT LQRMKRDWMHTGRRPSGLCGAALLVAARMHDF -> DSLRPASFPTWGCDLGVVTRVVT FT GVYPRCASRISVAGLCCLPSQEVLVCRMRGLHDMGVTVRDLWECGSPWQEGHLPMLGTV FT GC (in isoform 4)" FT /evidence="ECO:0000303|PubMed:10921893" FT /id="VSP_006399" FT VAR_SEQ 159..208 FT /note="NVYVLGKTFLLLARELCINAPAIDPCLYIPRFAHLLEFGEKNHEVSMTAL FT -> DSLRPASFPTWGCDLGVVTRVVTGVYPRCLHASQWPVCAACPVRKFWSVG (in FT isoform 6)" FT /evidence="ECO:0000303|PubMed:15489334" FT /id="VSP_043835" FT VAR_SEQ 209..677 FT /note="Missing (in isoform 6)" FT /evidence="ECO:0000303|PubMed:15489334" FT /id="VSP_043836" FT VAR_SEQ 243..677 FT /note="Missing (in isoform 4)" FT /evidence="ECO:0000303|PubMed:10921893" FT /id="VSP_006400" FT VAR_SEQ 293..338 FT /note="SYTAGQRKLRMKQLEQVLSKKLEEVEGEISSYQDAIEIELENSRPK -> IE FT EGGQTEAREPPQASSWEGPSTTRRRSQLWHGCPGCGRGGFTLCP (in isoform FT 2)" FT /evidence="ECO:0000303|PubMed:10921893, FT ECO:0000303|PubMed:15489334" FT /id="VSP_006397" FT VAR_SEQ 339..677 FT /note="Missing (in isoform 2)" FT /evidence="ECO:0000303|PubMed:10921893, FT ECO:0000303|PubMed:15489334" FT /id="VSP_006398" FT VAR_SEQ 459 FT /note="R -> RRDLSMPRCAKAKSQPHFPVLAQ (in isoform 8)" FT /evidence="ECO:0000303|PubMed:14702039" FT /id="VSP_045046" FT VARIANT 223 FT /note="R -> W (in CFDS; dbSNP:rs370270828)" FT /evidence="ECO:0000269|PubMed:25561519" FT /id="VAR_072710" FT VARIANT 226 FT /note="S -> L (in CFDS; dbSNP:rs606231416)" FT /evidence="ECO:0000269|PubMed:25561519" FT /id="VAR_072711" FT VARIANT 259 FT /note="T -> M (in CFDS; dbSNP:rs373957300)" FT /evidence="ECO:0000269|PubMed:25561519" FT /id="VAR_072712" FT VARIANT 292 FT /note="P -> H (in CFDS; dbSNP:rs606231450)" FT /evidence="ECO:0000269|PubMed:25561519" FT /id="VAR_072713" FT VARIANT 542 FT /note="V -> M (in a colorectal cancer sample; somatic FT mutation; dbSNP:rs371981699)" FT /evidence="ECO:0000269|PubMed:16959974" FT /id="VAR_035723" FT CONFLICT 88 FT /note="N -> D (in Ref. 1; AAC50170)" FT /evidence="ECO:0000305" FT CONFLICT 151 FT /note="D -> V (in Ref. 1; AAC50170)" FT /evidence="ECO:0000305" FT CONFLICT 224 FT /note="R -> G (in Ref. 1; AAC50170)" FT /evidence="ECO:0000305" FT CONFLICT 231 FT /note="A -> G (in Ref. 1; AAC50170)" FT /evidence="ECO:0000305" FT CONFLICT 339..340 FT /note="AK -> R (in Ref. 1; AAC50170)" FT /evidence="ECO:0000305" FT CONFLICT 437 FT /note="D -> N (in Ref. 4; BAH11919)" FT /evidence="ECO:0000305" FT CONFLICT 446 FT /note="E -> G (in Ref. 4; BAG53298)" FT /evidence="ECO:0000305" FT CONFLICT 594 FT /note="P -> T (in Ref. 1; AAC50170)" FT /evidence="ECO:0000305" FT CONFLICT 618 FT /note="G -> E (in Ref. 1; AAC50170)" FT /evidence="ECO:0000305" FT CONFLICT 640 FT /note="E -> G (in Ref. 4; BAG53298)" FT /evidence="ECO:0000305" SQ SEQUENCE 677 AA; 73840 MW; 5866304B879EC1DE CRC64; MTGRVCRGCG GTDIELDAAR GDAVCTACGS VLEDNIIVSE VQFVESSGGG SSAVGQFVSL DGAGKTPTLG GGFHVNLGKE SRAQTLQNGR RHIHHLGNQL QLNQHCLDTA FNFFKMAVSR HLTRGRKMAH VIAACLYLVC RTEGTPHMLL DLSDLLQVNV YVLGKTFLLL ARELCINAPA IDPCLYIPRF AHLLEFGEKN HEVSMTALRL LQRMKRDWMH TGRRPSGLCG AALLVAARMH DFRRTVKEVI SVVKVCESTL RKRLTEFEDT PTSQLTIDEF MKIDLEEECD PPSYTAGQRK LRMKQLEQVL SKKLEEVEGE ISSYQDAIEI ELENSRPKAK GGLASLAKDG STEDTASSLC GEEDTEDEEL EAAASHLNKD LYRELLGGAP GSSEAAGSPE WGGRPPALGS LLDPLPTAAS LGISDSIREC ISSQSSDPKD ASGDGELDLS GIDDLEIDRY ILNESEARVK AELWMRENAE YLREQREKEA RIAKEKELGI YKEHKPKKSC KRREPIQAST AREAIEKMLE QKKISSKINY SVLRGLSSAG GGSPHREDAQ PEHSASARKL SRRRTPASRS GADPVTSVGK RLRPLVSTQP AKKVATGEAL LPSSPTLGAE PARPQAVLVE SGPVSYHADE EADEEEPDEE DGEPCVSALQ MMGSNDYGCD GDEDDGY //