TF3B_MOUSE
ID TF3B_MOUSE Reviewed; 676 AA.
AC Q8CFK2;
DT 19-JUL-2005, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2003, sequence version 1.
DT 03-AUG-2022, entry version 129.
DE RecName: Full=Transcription factor IIIB 90 kDa subunit;
DE Short=TFIIIB90;
DE Short=mTFIIIB90;
DE AltName: Full=B-related factor 1;
DE Short=BRF-1;
GN Name=Brf1;
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=NMRI; TISSUE=Mammary tumor;
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 [2]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-365; SER-449 AND SER-552, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brown adipose tissue, Kidney, Lung, Pancreas, Spleen, and Testis;
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 which utilizes different
CC TFIIIB complexes at structurally distinct promoters. {ECO:0000250}.
CC -!- SUBUNIT: TFIIIB comprises at least the TATA-binding protein (TBP) and
CC the B-related factor 1 (BRF1/TFIIIB90). Interacts with BDP1 (By
CC similarity). Interacts with MAF1 (By similarity).
CC {ECO:0000250|UniProtKB:Q92994}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the TFIIB family. {ECO:0000305}.
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DR EMBL; BC037224; AAH37224.1; -; mRNA.
DR CCDS; CCDS49195.1; -.
DR AlphaFoldDB; Q8CFK2; -.
DR SMR; Q8CFK2; -.
DR STRING; 10090.ENSMUSP00000011302; -.
DR iPTMnet; Q8CFK2; -.
DR PhosphoSitePlus; Q8CFK2; -.
DR EPD; Q8CFK2; -.
DR jPOST; Q8CFK2; -.
DR MaxQB; Q8CFK2; -.
DR PaxDb; Q8CFK2; -.
DR PRIDE; Q8CFK2; -.
DR ProteomicsDB; 259015; -.
DR MGI; MGI:1919558; Brf1.
DR eggNOG; KOG1598; Eukaryota.
DR InParanoid; Q8CFK2; -.
DR PhylomeDB; Q8CFK2; -.
DR Reactome; R-MMU-76061; RNA Polymerase III Transcription Initiation From Type 1 Promoter.
DR Reactome; R-MMU-76066; RNA Polymerase III Transcription Initiation From Type 2 Promoter.
DR ChiTaRS; Brf1; mouse.
DR PRO; PR:Q8CFK2; -.
DR Proteomes; UP000000589; Unplaced.
DR RNAct; Q8CFK2; protein.
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; ISO:MGI.
DR GO; GO:0043488; P:regulation of mRNA stability; IMP:MGI.
DR GO; GO:0006383; P:transcription by RNA polymerase III; IBA:GO_Central.
DR GO; GO:0070897; P:transcription preinitiation complex assembly; IEA:InterPro.
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; Metal-binding; Nucleus; Phosphoprotein; Reference proteome;
KW Repeat; Transcription; Transcription regulation; Zinc; Zinc-finger.
FT CHAIN 1..676
FT /note="Transcription factor IIIB 90 kDa subunit"
FT /id="PRO_0000119348"
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 342..371
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 386..408
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 425..449
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 543..603
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 617..653
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 638..652
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:21183079"
FT MOD_RES 449
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 552
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
SQ SEQUENCE 676 AA; 73799 MW; 35110297F64E7E7C CRC64;
MTGRVCRGCG GTDIELDAAR GDAVCTGCGS VLEDNIIVSE VQFVENSGGG SSAVGQFVSL
DGAGKTPTLG GGFHVNLGKE SRAQTLQNGR RHIHHLGSQL QLNQHCLDTA FNFFKMAVSK
HLTRGRKMAH VIAACLYLVC RTEGTPHMLL DLSDLLQVNV YVLGKTFLLL ARELCINAPA
IDPCLYIPRF AHLLEFGEKN HEVSMTALRL LQRMKRDWMH TGRRPSGLCG AALLVAARMH
DFRRTVKEVI SVVKVCESTL RKRLTEFEDT PTSQLTIDEF MKIDLEEECD PPSYTAGQRK
LRMKQLEQVL SKKLEEVEGE ISSYQDAIEI ELENSRPKAK GALANLSKDG SGEDATSSPR
CEEDTEDEEL EAAASHMNKD FYRELLGDDD GSEAAGDPDG GSRPLALESL LGPLPTAASL
GISDSIRECI SSPSGDPKDS SGDGELDLSG IDDLEIDRYI LNESEARVKA ELWMRENAEY
LREQKEKEAR IAKEKELGIY KEHKPKKSCK RREPILASTA GEAIEKMLEQ KKISSKINYS
VLRDLNSKGG GSPPRDDSQP PERASTKKLS RRKRATTRNS ADPGTSTGKR LRPLLSAQPA
KKAAVGEALL LSSPALGAEP VKPSAVLVES GPVPYHPEED ADEEDAEDED GEPCVSALQM
MGGNDYGCDG DEDDGY
