ID TF2B_MOUSE Reviewed; 316 AA. AC P62915; P29053; DT 31-AUG-2004, integrated into UniProtKB/Swiss-Prot. DT 31-AUG-2004, sequence version 1. DT 27-MAR-2024, entry version 155. DE RecName: Full=Transcription initiation factor IIB {ECO:0000250|UniProtKB:Q00403}; DE EC=2.3.1.48 {ECO:0000250|UniProtKB:Q00403}; DE AltName: Full=General transcription factor TFIIB {ECO:0000250|UniProtKB:Q00403}; DE AltName: Full=RNA polymerase II alpha initiation factor; GN Name=Gtf2b {ECO:0000312|MGI:MGI:2385191}; 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]. 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 INTERACTION WITH GPBP1. RX PubMed=14612417; DOI=10.1128/mcb.23.23.8773-8785.2003; RA Hsu L.-C., Liu S., Abedinpour F., Beech R.D., Lahti J.M., Kidd V.J., RA Greenspan J.A., Yeung C.-Y.; RT "The murine G+C-rich promoter binding protein mGPBP is required for RT promoter-specific transcription."; RL Mol. Cell. Biol. 23:8773-8785(2003). RN [3] RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Brain, Kidney, Liver, Lung, 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 transcription factor that plays a role in CC transcription initiation by RNA polymerase II (Pol II). Involved in the CC pre-initiation complex (PIC) formation and Pol II recruitment at CC promoter DNA. Together with the TATA box-bound TBP forms the core CC initiation complex and provides a bridge between TBP and the Pol II- CC TFIIF complex. Released from the PIC early following the onset of CC transcription during the initiation and elongation transition and CC reassociates with TBP during the next transcription cycle. Associates CC with chromatin to core promoter-specific regions. Binds to two distinct CC DNA core promoter consensus sequence elements in a TBP-independent CC manner; these IIB-recognition elements (BREs) are localized immediately CC upstream (BREu), 5'-[GC][GC][GA]CGCC-3', and downstream (BREd), 5'- CC [GA]T[TGA][TG][GT][TG][TG]-3', of the TATA box element. Modulates CC transcription start site selection. Exhibits also autoacetyltransferase CC activity that contributes to the activated transcription. CC {ECO:0000250|UniProtKB:Q00403}. CC -!- CATALYTIC ACTIVITY: CC Reaction=acetyl-CoA + L-lysyl-[protein] = CoA + H(+) + N(6)-acetyl-L- CC lysyl-[protein]; Xref=Rhea:RHEA:45948, Rhea:RHEA-COMP:9752, CC Rhea:RHEA-COMP:10731, ChEBI:CHEBI:15378, ChEBI:CHEBI:29969, CC ChEBI:CHEBI:57287, ChEBI:CHEBI:57288, ChEBI:CHEBI:61930; EC=2.3.1.48; CC Evidence={ECO:0000250|UniProtKB:Q00403}; CC -!- SUBUNIT: Found in a ternary complex with TATA box-bound TBP. Part of a CC TFIID-containing RNA polymerase II pre-initiation complex (PIC) that is CC composed of TBP and at least GTF2A1, GTF2A2, GTF2E1, GTF2E2, GTF2F1, CC GTF2H2, GTF2H3, GTF2H4, GTF2H5, GTF2B, TCEA1, ERCC2, ERCC3, TAF1, TAF2, CC TAF3, TAF4, TAF5, TAF6, TAF7, TAF8, TAF9, TAF10, TAF11, TAF12 and CC TAF13. Associates with TFIID-TFIIA (DA complex) to form TFIID-TFIIA- CC TFIIB (DAB complex), which is then recognized by RNA polymerase II (Pol CC II). Found in a RNA polymerase II initiation complex. Interacts (via C- CC terminus) with TBP; this interaction with TATA box-bound TBP guides Pol CC II into the PIC. Interacts (via N-terminus) with Pol II. Interacts (via CC C-terminus) with SSU72; this interaction is inhibited by SYMPK. CC Interacts with NR2F1; this interaction is direct. Interacts with PGR. CC Interacts with ESR1. Interacts with GTF2F1 (via C-terminus and CC preferentially via acetylated form); this interaction prevents binding CC of GTF2B to GTF2F2. Interacts with GTF2F2 (via N-terminus); this CC interaction is inhibited in presence of GTF2F1. Interacts with the CC transcription elongation factor TCEA2. Interacts with HSF1 (via CC transactivation domain) (By similarity). Interacts with GPBP1 CC (PubMed:14612417). {ECO:0000250|UniProtKB:Q00403, CC ECO:0000269|PubMed:14612417}. CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:Q00403}. CC Chromosome {ECO:0000250|UniProtKB:Q00403}. Note=Non-acetylated form CC colocalizes with DNA in the G0/1, S and G2 phases of the cell cycle, CC but not during mitosis. Acetylated form colocalizes at CC transcriptionally silent mitotic chromatids during mitosis at CC metaphase, anaphase, and telophase phases of the cell cycle. CC {ECO:0000250|UniProtKB:Q00403}. CC -!- DOMAIN: The TFIIB-type zinc-binding domain is necessary for the CC interaction and recruitment of RNA polymerase II to the core promoter, CC the formation of a fully competent pre-initiation complex (PIC) CC assembly and basal transcription initiation. The C-terminus is CC necessary and sufficient for interaction with the TATA box-bound TBP CC complex and for the formation of PIC. {ECO:0000250|UniProtKB:Q00403}. CC -!- PTM: Acetylated. Autoacetylated; autoacetylation at Lys-238 stimulates CC transcription activation. {ECO:0000250|UniProtKB:Q00403}. CC -!- SIMILARITY: Belongs to the TFIIB family. {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; BC016637; AAH16637.1; -; mRNA. DR CCDS; CCDS17882.1; -. DR RefSeq; NP_663521.1; NM_145546.1. DR PDB; 8D5E; X-ray; 2.46 A; P=88-96. DR PDB; 8D5F; X-ray; 2.31 A; P=88-96. DR PDBsum; 8D5E; -. DR PDBsum; 8D5F; -. DR AlphaFoldDB; P62915; -. DR SMR; P62915; -. DR BioGRID; 230917; 26. DR IntAct; P62915; 13. DR STRING; 10090.ENSMUSP00000029938; -. DR iPTMnet; P62915; -. DR PhosphoSitePlus; P62915; -. DR SwissPalm; P62915; -. DR EPD; P62915; -. DR PaxDb; 10090-ENSMUSP00000029938; -. DR PeptideAtlas; P62915; -. DR ProteomicsDB; 263035; -. DR Pumba; P62915; -. DR Antibodypedia; 19819; 518 antibodies from 36 providers. DR DNASU; 229906; -. DR Ensembl; ENSMUST00000029938.10; ENSMUSP00000029938.9; ENSMUSG00000028271.10. DR GeneID; 229906; -. DR KEGG; mmu:229906; -. DR UCSC; uc008rpb.1; mouse. DR AGR; MGI:2385191; -. DR CTD; 2959; -. DR MGI; MGI:2385191; Gtf2b. DR VEuPathDB; HostDB:ENSMUSG00000028271; -. DR eggNOG; KOG1597; Eukaryota. DR GeneTree; ENSGT00390000006671; -. DR HOGENOM; CLU_043736_1_1_1; -. DR InParanoid; P62915; -. DR OMA; DHDQRMK; -. DR OrthoDB; 38673at2759; -. DR PhylomeDB; P62915; -. DR TreeFam; TF105953; -. DR Reactome; R-MMU-674695; RNA Polymerase II Pre-transcription Events. DR Reactome; R-MMU-6807505; RNA polymerase II transcribes snRNA genes. DR Reactome; R-MMU-73776; RNA Polymerase II Promoter Escape. DR Reactome; R-MMU-73779; RNA Polymerase II Transcription Pre-Initiation And Promoter Opening. DR Reactome; R-MMU-75953; RNA Polymerase II Transcription Initiation. DR Reactome; R-MMU-76042; RNA Polymerase II Transcription Initiation And Promoter Clearance. DR BioGRID-ORCS; 229906; 28 hits in 76 CRISPR screens. DR ChiTaRS; Gtf2b; mouse. DR PRO; PR:P62915; -. DR Proteomes; UP000000589; Chromosome 3. DR RNAct; P62915; Protein. DR Bgee; ENSMUSG00000028271; Expressed in primary oocyte and 269 other cell types or tissues. DR ExpressionAtlas; P62915; baseline and differential. DR GO; GO:0032153; C:cell division site; IDA:MGI. DR GO; GO:0005694; C:chromosome; ISS:UniProtKB. DR GO; GO:0000793; C:condensed chromosome; IDA:MGI. DR GO; GO:0042585; C:germinal vesicle; IDA:MGI. DR GO; GO:0000776; C:kinetochore; IDA:MGI. DR GO; GO:0016604; C:nuclear body; ISO:MGI. DR GO; GO:0005654; C:nucleoplasm; ISO:MGI. DR GO; GO:0005634; C:nucleus; IDA:MGI. DR GO; GO:0032993; C:protein-DNA complex; ISS:UniProtKB. DR GO; GO:0090575; C:RNA polymerase II transcription regulator complex; ISO:MGI. DR GO; GO:0005669; C:transcription factor TFIID complex; ISO:MGI. DR GO; GO:0097550; C:transcription preinitiation complex; IBA:GO_Central. DR GO; GO:0016407; F:acetyltransferase activity; ISS:UniProtKB. DR GO; GO:0003677; F:DNA binding; IDA:MGI. DR GO; GO:0140297; F:DNA-binding transcription factor binding; ISO:MGI. DR GO; GO:0004402; F:histone acetyltransferase activity; IEA:UniProtKB-EC. DR GO; GO:0046966; F:nuclear thyroid hormone receptor binding; ISO:MGI. DR GO; GO:1990841; F:promoter-specific chromatin binding; IDA:MGI. DR GO; GO:0000993; F:RNA polymerase II complex binding; ISS:UniProtKB. DR GO; GO:0000979; F:RNA polymerase II core promoter sequence-specific DNA binding; ISO:MGI. DR GO; GO:0016251; F:RNA polymerase II general transcription initiation factor activity; ISO:MGI. DR GO; GO:0017025; F:TBP-class protein binding; ISO:MGI. DR GO; GO:0008270; F:zinc ion binding; ISS:UniProtKB. DR GO; GO:0051276; P:chromosome organization; IMP:MGI. DR GO; GO:0010467; P:gene expression; IMP:MGI. DR GO; GO:0051177; P:meiotic sister chromatid cohesion; IMP:MGI. DR GO; GO:0006473; P:protein acetylation; ISS:UniProtKB. DR GO; GO:1990114; P:RNA polymerase II core complex assembly; ISS:UniProtKB. DR GO; GO:0051123; P:RNA polymerase II preinitiation complex assembly; ISS:UniProtKB. DR GO; GO:0051225; P:spindle assembly; IMP:MGI. DR GO; GO:0006366; P:transcription by RNA polymerase II; ISS:UniProtKB. DR GO; GO:0006367; P:transcription initiation at RNA polymerase II promoter; ISS:UniProtKB. DR GO; GO:0001174; P:transcriptional start site selection at RNA polymerase II promoter; ISS:UniProtKB. DR GO; GO:0019083; P:viral transcription; ISS:UniProtKB. DR CDD; cd20551; CYCLIN_TFIIB_rpt1; 1. DR CDD; cd20552; CYCLIN_TFIIB_rpt2; 1. DR Gene3D; 2.20.25.10; -; 1. DR Gene3D; 1.10.472.10; Cyclin-like; 2. DR InterPro; IPR013763; Cyclin-like_dom. DR InterPro; IPR036915; Cyclin-like_sf. DR InterPro; IPR000812; TFIIB. DR InterPro; IPR023486; TFIIB_CS. DR InterPro; IPR013150; TFIIB_cyclin. DR InterPro; IPR013137; Znf_TFIIB. DR PANTHER; PTHR11618:SF13; TRANSCRIPTION INITIATION FACTOR IIB; 1. DR PANTHER; PTHR11618; TRANSCRIPTION INITIATION FACTOR IIB-RELATED; 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; PS00782; TFIIB; 2. DR PROSITE; PS51134; ZF_TFIIB; 1. DR Genevisible; P62915; MM. PE 1: Evidence at protein level; KW 3D-structure; Acetylation; Acyltransferase; Chromosome; DNA-binding; KW Metal-binding; Nucleus; Phosphoprotein; Reference proteome; Repeat; KW Transcription; Transcription regulation; Transferase; Zinc; Zinc-finger. FT CHAIN 1..316 FT /note="Transcription initiation factor IIB" FT /id="PRO_0000119294" FT REPEAT 124..200 FT /note="1" FT REPEAT 218..294 FT /note="2" FT ZN_FING 11..42 FT /note="TFIIB-type" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00469" FT REGION 189..193 FT /note="Core promoter DNA-binding" FT /evidence="ECO:0000250|UniProtKB:Q00403" FT REGION 244..316 FT /note="Necessary for TATA box-bound TBP complex formation" FT /evidence="ECO:0000250|UniProtKB:Q00403" FT REGION 249..252 FT /note="Core promoter DNA-binding" FT /evidence="ECO:0000250|UniProtKB:Q00403" FT REGION 283..286 FT /note="Core promoter DNA-binding" FT /evidence="ECO:0000250|UniProtKB:Q00403" FT BINDING 15 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00469" FT BINDING 18 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00469" FT BINDING 34 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00469" FT BINDING 37 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00469" FT BINDING 152 FT /ligand="DNA" FT /ligand_id="ChEBI:CHEBI:16991" FT /evidence="ECO:0000250|UniProtKB:Q00403" FT BINDING 154 FT /ligand="DNA" FT /ligand_id="ChEBI:CHEBI:16991" FT /evidence="ECO:0000250|UniProtKB:Q00403" FT BINDING 189 FT /ligand="DNA" FT /ligand_id="ChEBI:CHEBI:16991" FT /evidence="ECO:0000250|UniProtKB:Q00403" FT BINDING 196 FT /ligand="DNA" FT /ligand_id="ChEBI:CHEBI:16991" FT /evidence="ECO:0000250|UniProtKB:Q00403" FT BINDING 248 FT /ligand="DNA" FT /ligand_id="ChEBI:CHEBI:16991" FT /evidence="ECO:0000250|UniProtKB:Q00403" FT BINDING 272 FT /ligand="DNA" FT /ligand_id="ChEBI:CHEBI:16991" FT /evidence="ECO:0000250|UniProtKB:Q00403" FT BINDING 281 FT /ligand="DNA" FT /ligand_id="ChEBI:CHEBI:16991" FT /evidence="ECO:0000250|UniProtKB:Q00403" FT BINDING 284 FT /ligand="DNA" FT /ligand_id="ChEBI:CHEBI:16991" FT /evidence="ECO:0000250|UniProtKB:Q00403" FT BINDING 286 FT /ligand="DNA" FT /ligand_id="ChEBI:CHEBI:16991" FT /evidence="ECO:0000250|UniProtKB:Q00403" FT BINDING 290 FT /ligand="DNA" FT /ligand_id="ChEBI:CHEBI:16991" FT /evidence="ECO:0000250|UniProtKB:Q00403" FT MOD_RES 70 FT /note="Phosphoserine" FT /evidence="ECO:0000250|UniProtKB:Q00403" FT MOD_RES 76 FT /note="Phosphoserine" FT /evidence="ECO:0000250|UniProtKB:Q00403" FT MOD_RES 92 FT /note="Phosphoserine" FT /evidence="ECO:0000250|UniProtKB:Q00403" FT MOD_RES 238 FT /note="N6-acetyllysine; by autocatalysis" FT /evidence="ECO:0000250|UniProtKB:Q00403" SQ SEQUENCE 316 AA; 34819 MW; 9CC7E102526C21F9 CRC64; MASTSRLDAL PRVTCPNHPD AILVEDYRAG DMICPECGLV VGDRVIDVGS EWRTFSNDKA TKDPSRVGDS QNPLLSDGDL STMIGKGTGA ASFDEFGNSK YQNRRTMSSS DRAMMNAFKE ITTMADRINL PRNIVDRTNN LFKQVYEQKS LKGRANDAIA SACLYIACRQ EGVPRTFKEI CAVSRISKKE IGRCFKLILK ALETSVDLIT TGDFMSRFCS NLCLPKQVQM AATHIARKAV ELDLVPGRSP ISVAAAAIYM ASQASAEKRT QKEIGDIAGV ADVTIRQSYR LIYPRAPDLF PSDFKFDTPV DKLPQL //