TF3B_HUMAN
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 03-AUG-2022, entry version 187.
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};
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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; 85.
DR CORUM; Q92994; -.
DR IntAct; Q92994; 12.
DR MINT; Q92994; -.
DR STRING; 9606.ENSP00000448323; -.
DR ChEMBL; CHEMBL4523421; -.
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; Q92994; -.
DR PeptideAtlas; Q92994; -.
DR PRIDE; 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 Antibodypedia; 14980; 260 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 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; 412601at2759; -.
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; 770 hits in 1085 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 127 other tissues.
DR ExpressionAtlas; Q92994; baseline and differential.
DR Genevisible; Q92994; HS.
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 from 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; cd00043; CYCLIN; 2.
DR InterPro; IPR029529; Brf1.
DR InterPro; IPR011665; BRF1_TBP-bd_dom.
DR InterPro; IPR013763; Cyclin-like.
DR InterPro; IPR036915; Cyclin-like_sf.
DR InterPro; IPR000812; TFIIB.
DR InterPro; IPR013150; TFIIB_cyclin.
DR InterPro; IPR013137; Znf_TFIIB.
DR PANTHER; PTHR11618; PTHR11618; 1.
DR PANTHER; PTHR11618:SF4; PTHR11618:SF4; 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; SSF47954; 2.
DR PROSITE; PS51134; ZF_TFIIB; 1.
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
