ID TF2B_PONAB Reviewed; 316 AA.
AC Q5R886;
DT 19-JUL-2005, integrated into UniProtKB/Swiss-Prot.
DT 21-DEC-2004, sequence version 1.
DT 27-MAR-2024, entry version 110.
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};
GN Name=GTF2B {ECO:0000250|UniProtKB:Q00403};
OS Pongo abelii (Sumatran orangutan) (Pongo pygmaeus abelii).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Pongo.
OX NCBI_TaxID=9601;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Heart;
RG The German cDNA consortium;
RL Submitted (NOV-2004) to the EMBL/GenBank/DDBJ databases.
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 (By
CC similarity). {ECO:0000250|UniProtKB:P62915,
CC ECO:0000250|UniProtKB:Q00403}.
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}.
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DR EMBL; CR859868; CAH92024.1; -; mRNA.
DR RefSeq; NP_001126175.1; NM_001132703.1.
DR AlphaFoldDB; Q5R886; -.
DR SMR; Q5R886; -.
DR STRING; 9601.ENSPPYP00000001365; -.
DR Ensembl; ENSPPYT00000001410.3; ENSPPYP00000001365.3; ENSPPYG00000001178.3.
DR GeneID; 100173138; -.
DR KEGG; pon:100173138; -.
DR CTD; 2959; -.
DR eggNOG; KOG1597; Eukaryota.
DR GeneTree; ENSGT00390000006671; -.
DR HOGENOM; CLU_043736_1_1_1; -.
DR InParanoid; Q5R886; -.
DR OMA; DHDQRMK; -.
DR OrthoDB; 38673at2759; -.
DR Proteomes; UP000001595; Chromosome 1.
DR GO; GO:0032153; C:cell division site; IEA:Ensembl.
DR GO; GO:0005694; C:chromosome; ISS:UniProtKB.
DR GO; GO:0042585; C:germinal vesicle; IEA:Ensembl.
DR GO; GO:0000776; C:kinetochore; IEA:Ensembl.
DR GO; GO:0016604; C:nuclear body; IEA:Ensembl.
DR GO; GO:0005634; C:nucleus; ISS:UniProtKB.
DR GO; GO:0032993; C:protein-DNA complex; ISS:UniProtKB.
DR GO; GO:0005669; C:transcription factor TFIID complex; IEA:Ensembl.
DR GO; GO:0016407; F:acetyltransferase activity; ISS:UniProtKB.
DR GO; GO:0004402; F:histone acetyltransferase activity; IEA:UniProtKB-EC.
DR GO; GO:0046966; F:nuclear thyroid hormone receptor binding; IEA:Ensembl.
DR GO; GO:1990841; F:promoter-specific chromatin binding; ISS:UniProtKB.
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; ISS:UniProtKB.
DR GO; GO:0016251; F:RNA polymerase II general transcription initiation factor activity; IEA:Ensembl.
DR GO; GO:0017025; F:TBP-class protein binding; IEA:Ensembl.
DR GO; GO:0008270; F:zinc ion binding; ISS:UniProtKB.
DR GO; GO:0051177; P:meiotic sister chromatid cohesion; IEA:Ensembl.
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; IEA:Ensembl.
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.
PE 2: Evidence at transcript level;
KW Acetylation; Acyltransferase; Chromosome; DNA-binding; Metal-binding;
KW Nucleus; Phosphoprotein; Reference proteome; Repeat; Transcription;
KW Transcription regulation; Transferase; Zinc; Zinc-finger.
FT CHAIN 1..316
FT /note="Transcription initiation factor IIB"
FT /id="PRO_0000119295"
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 complex TBP 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; 34833 MW; 9CC7E102526C2722 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
PTDFKFDTPV DKLPQL
//
