BRF2_MOUSE
ID BRF2_MOUSE Reviewed; 420 AA.
AC Q3UAW9; Q9CZF0;
DT 20-MAY-2008, integrated into UniProtKB/Swiss-Prot.
DT 11-OCT-2005, sequence version 1.
DT 03-AUG-2022, entry version 113.
DE RecName: Full=Transcription factor IIIB 50 kDa subunit;
DE AltName: Full=B-related factor 2;
DE Short=BRF-2;
GN Name=Brf2;
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J; TISSUE=Bone marrow;
RX PubMed=16141072; DOI=10.1126/science.1112014;
RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT "The transcriptional landscape of the mammalian genome.";
RL Science 309:1559-1563(2005).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=Czech II; TISSUE=Lung;
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 [3]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Kidney, and Spleen;
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
CC -!- FUNCTION: General activator of RNA polymerase III transcription. Factor
CC exclusively required for RNA polymerase III transcription of genes with
CC promoter elements upstream of the initiation sites. Contributes to the
CC regulation of gene expression; functions as activator in the absence of
CC oxidative stress. Down-regulates expression of target genes in response
CC to oxidative stress. Overexpression protects cells against apoptosis in
CC response to oxidative stress. {ECO:0000250|UniProtKB:Q9HAW0}.
CC -!- SUBUNIT: Component of TFIIIB complexes. The TFIIIB complex has two
CC activities, alpha and beta. The TFIIIB-alpha activity complex is
CC composed of TBP, BDP1, and a complex containing both BRF2 and at least
CC four stably associated proteins; this complex inhibits the
CC transcription by pol III via its phosphorylation by CK2; YY1
CC facilitates the TFIIIB-alpha complex formation. Interacts with TBP;
CC this interaction promotes recruitment of BRF2 to TATA box-containing
CC promoters. Interacts with TBP and the BURE sequence (GC-rich sequence
CC downstream from the TATA box) to form a strong ternary complex which is
CC joined by BDP1; this ternary complex stimulates pol III transcription.
CC Forms a trimeric complex composed of TBP, BRF2 and mini-SNAPc complex
CC (SNAP43, SNAP50, and the N-terminal third of SNAP190) on the promoter.
CC Assembly of the TBP-BRF2 complex is stimulated by SNAP190. Interacts
CC with MAF1 and SNAPC4. {ECO:0000250|UniProtKB:Q9HAW0}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:Q9HAW0}.
CC -!- PTM: In response to oxidative stress, Cys-362 is reversibly oxidized to
CC cysteine sulfenic acid. Oxidation of Cys-362 impairs formation of a
CC ternary complex with TBP and DNA and down-regulates expression of
CC target genes in response to oxidative stress.
CC {ECO:0000250|UniProtKB:Q9HAW0}.
CC -!- SIMILARITY: Belongs to the TFIIB family. {ECO:0000305}.
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DR EMBL; AK012680; BAB28406.1; -; mRNA.
DR EMBL; AK028228; BAC25827.1; -; mRNA.
DR EMBL; AK151198; BAE30195.1; -; mRNA.
DR EMBL; BC098232; AAH98232.1; -; mRNA.
DR CCDS; CCDS22211.1; -.
DR RefSeq; NP_079962.1; NM_025686.2.
DR AlphaFoldDB; Q3UAW9; -.
DR SMR; Q3UAW9; -.
DR STRING; 10090.ENSMUSP00000033877; -.
DR iPTMnet; Q3UAW9; -.
DR PhosphoSitePlus; Q3UAW9; -.
DR PaxDb; Q3UAW9; -.
DR PRIDE; Q3UAW9; -.
DR ProteomicsDB; 273702; -.
DR DNASU; 66653; -.
DR GeneID; 66653; -.
DR KEGG; mmu:66653; -.
DR UCSC; uc009lhy.1; mouse.
DR CTD; 55290; -.
DR MGI; MGI:1913903; Brf2.
DR eggNOG; KOG1598; Eukaryota.
DR InParanoid; Q3UAW9; -.
DR OrthoDB; 1518547at2759; -.
DR PhylomeDB; Q3UAW9; -.
DR TreeFam; TF331596; -.
DR Reactome; R-MMU-76071; RNA Polymerase III Transcription Initiation From Type 3 Promoter.
DR BioGRID-ORCS; 66653; 22 hits in 71 CRISPR screens.
DR ChiTaRS; Brf2; mouse.
DR PRO; PR:Q3UAW9; -.
DR Proteomes; UP000000589; Unplaced.
DR RNAct; Q3UAW9; protein.
DR GO; GO:0005634; C:nucleus; IBA:GO_Central.
DR GO; GO:0000126; C:transcription factor TFIIIB complex; ISS:UniProtKB.
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:0001006; F:RNA polymerase III type 3 promoter sequence-specific DNA binding; ISS:UniProtKB.
DR GO; GO:0017025; F:TBP-class protein binding; IBA:GO_Central.
DR GO; GO:0034599; P:cellular response to oxidative stress; ISS:UniProtKB.
DR GO; GO:0006352; P:DNA-templated transcription, initiation; IBA:GO_Central.
DR GO; GO:0006359; P:regulation of transcription by RNA polymerase III; ISS:UniProtKB.
DR GO; GO:0070897; P:transcription preinitiation complex assembly; IEA:InterPro.
DR InterPro; IPR036915; Cyclin-like_sf.
DR InterPro; IPR000812; TFIIB.
DR InterPro; IPR013137; Znf_TFIIB.
DR PANTHER; PTHR11618; PTHR11618; 1.
DR Pfam; PF08271; TF_Zn_Ribbon; 1.
DR SUPFAM; SSF47954; SSF47954; 1.
DR PROSITE; PS51134; ZF_TFIIB; 1.
PE 1: Evidence at protein level;
KW Activator; Metal-binding; Nucleus; Oxidation; Phosphoprotein;
KW Reference proteome; Repeat; Transcription; Transcription regulation; Zinc;
KW Zinc-finger.
FT CHAIN 1..420
FT /note="Transcription factor IIIB 50 kDa subunit"
FT /id="PRO_0000337189"
FT REPEAT 72..157
FT /note="1"
FT REPEAT 173..249
FT /note="2"
FT ZN_FING 3..36
FT /note="TFIIB-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00469"
FT REGION 108..114
FT /note="Interaction with target DNA"
FT /evidence="ECO:0000250|UniProtKB:Q9HAW0"
FT REGION 316..387
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 358..364
FT /note="Required for the formation of a ternary complex with
FT DNA and TBP; not required for interaction with TBP in the
FT absence of DNA"
FT /evidence="ECO:0000250|UniProtKB:Q9HAW0"
FT REGION 366..420
FT /note="Required for interaction with TBP and formation of a
FT ternary complex with DNA and TBP"
FT /evidence="ECO:0000250|UniProtKB:Q9HAW0"
FT COMPBIAS 316..336
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 7
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00469"
FT BINDING 10
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 BINDING 31
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00469"
FT MOD_RES 354
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9HAW0"
FT MOD_RES 362
FT /note="Cysteine sulfenic acid (-SOH)"
FT /evidence="ECO:0000250|UniProtKB:Q9HAW0"
FT CONFLICT 352
FT /note="R -> P (in Ref. 1; BAB28406/BAC25827 and 2;
FT AAH98232)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 420 AA; 47050 MW; 9B1D662EF90302F8 CRC64;
MPNGSRCPDC GSSELVEDSH YSQSQLVCSD CGCVVTEGVL TTTFSDEGNF REVTYSRSTG
ENEQVSRCQQ RDLRRVRDLC RILKLPLTFE DTAISYYQKA YQLSGIRAAR LQKKEVLVGC
CVLITCRQHN WPLTMGTICT LLYADLDLFS GTYMQMVKLL GLDVPSLCLA DLVKSYCSSF
KLFQASPSVP AKYVEDKDKM LSRTLLLVEL ADETWLVTGR HPLPIITAAT FLAWQSLRPS
DRLTCSLAQF CKLANVDLPY PAASRLQELL AVLLQMAGQL AWLQVLKLNK RSVVKHIGDL
LQHRHMLVRT AFRDGTAEVE TQQQQQQQQG QGQGQQDEVG DGPFDLPKRK RRASPTPLLP
PCMLKPPKRT HTLPPESAVT GDEDISDSEI EQYLRTPQEV RDFERAQAAS QAAMRVPNPP
