GTF2B
entrez
2959
canonical
uniprot
Q00403
canonical
ensembl
ENSG00000137947
resolver
ensp
ENSP00000359531
resolver
enst
ENST00000370500
resolver
genesymbol
GTF2B
resolver
genesymbol_syn
TF2B
resolver
genesymbol_syn
TFIIB
resolver
hgnc
HGNC:4648
resolver
uniprot
A8K1A7
resolver
uniprot
Q5JS30
resolver
uniprot_entry
TF2B_HUMAN
resolver
uniprot_sec
A8K1A7
resolver
uniprot_sec
Q5JS30
resolver
amino_acid_sequence
MASTSRLDALPRVTCPNHPDAILVEDYRAGDMICPECGLVVGDRVIDVGSEWRTFSNDKATKDPSRVGDSQNPLLSDGDLSTMIGKGTGAASFDEFGNSKYQNRRTMSSSDRAMMNAFKEITTMADRINLPRNIVDRTNNLFKQVYEQKSLKGRANDAIASACLYIACRQEGVPRTFKEICAVSRISKKEIGRCFKLILKALETSVDLITTGDFMSRFCSNLCLPKQVQMAATHIARKAVELDLVPGRSPISVAAAAIYMASQASAEKRTQKEIGDIAGVADVTIRQSYRLIYPRAPDLFPTDFKFDTPVDKLPQL
uniprot
proteins
ec_number
2.3.1.48
uniprot
proteins
function
FUNCTION: General transcription factor that plays a role in transcription initiation by RNA polymerase II (Pol II). Involved in the pre-initiation complex (PIC) formation and Pol II recruitment at promoter DNA (PubMed:12931194, PubMed:1517211, PubMed:1876184, PubMed:1946368, PubMed:27193682, PubMed:3029109, PubMed:3818643, PubMed:7601352, PubMed:8413225, PubMed:8515820, PubMed:8516311, PubMed:8516312, PubMed:9420329). Together with the TATA box-bound TBP forms the core initiation complex and provides a bridge between TBP and the Pol II-TFIIF complex (PubMed:8413225, PubMed:8504927, PubMed:8515820, PubMed:8516311, PubMed:8516312). Released from the PIC early following the onset of transcription during the initiation and elongation transition and reassociates with TBP during the next transcription cycle (PubMed:7601352). Associates with chromatin to core promoter-specific regions (PubMed:12931194, PubMed:24441171). Binds to two distinct DNA core promoter consensus sequence elements in a TBP-independent manner; these IIB-recognition elements (BREs) are localized immediately upstream (BREu), 5'-[GC][GC][GA]CGCC-3', and downstream (BREd), 5'-[GA]T[TGA][TG][GT][TG][TG]-3', of the TATA box element (PubMed:10619841, PubMed:16230532, PubMed:7675079, PubMed:9420329). Modulates transcription start site selection (PubMed:10318856). Also exhibits autoacetyltransferase activity that contributes to the activated transcription (PubMed:12931194). {ECO:0000269|PubMed:10318856, ECO:0000269|PubMed:10619841, ECO:0000269|PubMed:12931194, ECO:0000269|PubMed:1517211, ECO:0000269|PubMed:16230532, ECO:0000269|PubMed:1876184, ECO:0000269|PubMed:1946368, ECO:0000269|PubMed:24441171, ECO:0000269|PubMed:27193682, ECO:0000269|PubMed:3029109, ECO:0000269|PubMed:3818643, ECO:0000269|PubMed:7601352, ECO:0000269|PubMed:7675079, ECO:0000269|PubMed:8413225, ECO:0000269|PubMed:8504927, ECO:0000269|PubMed:8515820, ECO:0000269|PubMed:8516311, ECO:0000269|PubMed:8516312, ECO:0000269|PubMed:9420329}.
uniprot
proteins
mass_dalton
34833
uniprot
proteins
mutagenesis
MUTAGEN 37; /note="C->S: Does not inhibit interaction with TBP. Inhibits the recruitment of RNA polymerase II into the initiation complex."; /evidence="ECO:0000269|PubMed:8516312"; MUTAGEN 51..56; /note="EWRTFS->AWRTFA: Partial loss of HIV-1 Vpr binding."; /evidence="ECO:0000269|PubMed:10359081"; MUTAGEN 51; /note="E->R,A,D: Defects in transcription start site selection. Supports a level of transcription equivalent to wild-type."; /evidence="ECO:0000269|PubMed:10318856"; MUTAGEN 52; /note="W->A: Partial loss of HIV-1 Vpr binding."; /evidence="ECO:0000269|PubMed:10359081"; MUTAGEN 53..54; /note="RT->AA: Partial loss of HIV-1 Vpr binding."; /evidence="ECO:0000269|PubMed:10359081"; MUTAGEN 55; /note="F->A: Partial loss of HIV-1 Vpr binding."; /evidence="ECO:0000269|PubMed:10359081"; MUTAGEN 66; /note="R->A,E,K: Defects in transcription start site selection. Supports a level of transcription equivalent to wild-type."; /evidence="ECO:0000269|PubMed:10318856"; MUTAGEN 153; /note="G->Q: Decreases BREd-dependent pre-initiation complex formation."; /evidence="ECO:0000269|PubMed:16230532"; MUTAGEN 185; /note="R->E: Reduces interaction with SSU72; when associated with E-193 or E-200. Inhibits interaction with VP16; when associated with E-193. Inhibits RNA pol II transcription activation induced by VP16 but does not affect basal transcription; when associated with E-193."; /evidence="ECO:0000269|PubMed:29158257, ECO:0000269|PubMed:8515819"; MUTAGEN 185; /note="R->L: Reduces interaction with VP16; when associated with L-189."; /evidence="ECO:0000269|PubMed:8515819"; MUTAGEN 189; /note="K->E: Inhibits interaction with SSU72; when associated with E-193. Reduces interaction with SSU72; when associated with E-200. Inhibits interaction with VP16; when associated with E-200. Inhibits RNA pol II transcription activation induced by VP16 but does not affect basal transcription; when associated with E-200."; /evidence="ECO:0000269|PubMed:29158257, ECO:0000269|PubMed:8515819"; MUTAGEN 189; /note="K->L: Reduces interaction with VP16; when associated with L-185."; /evidence="ECO:0000269|PubMed:8515819"; MUTAGEN 193; /note="R->E: Inhibits interaction with SSU72; when associated with E-185 or E-189. Inhibits interaction with VP16; when associated with E-185. Inhibits RNA pol II transcription activation induced by VP16 but does not affect basal transcription; when associated with E-185."; /evidence="ECO:0000269|PubMed:29158257, ECO:0000269|PubMed:8515819"; MUTAGEN 196; /note="K->L: Reduces interaction with VP16; when associated with L-200."; /evidence="ECO:0000269|PubMed:8515819"; MUTAGEN 200..208; /note="KALETSVDL->GSGS: Reduces the formation of the TATA box-bound TBP ternary complex."; /evidence="ECO:0000269|PubMed:29158257"; MUTAGEN 200; /note="K->E: Reduces interaction with SSU72; when associated with E-185 or E-189. Inhibits interaction with VP16; when associated with E-189. Inhibits RNA pol II transcription activation induced by VP16 but does not affect basal transcription; when associated with E-189."; /evidence="ECO:0000269|PubMed:29158257, ECO:0000269|PubMed:8515819"; MUTAGEN 200; /note="K->KGSGS: Reduces the formation of the TATA box-bound TBP ternary complex."; /evidence="ECO:0000269|PubMed:29158257"; MUTAGEN 200; /note="K->L: Reduces interaction with VP16; when associated with L-196."; /evidence="ECO:0000269|PubMed:8515819"; MUTAGEN 208; /note="L->LGSGS: Does not inhibit the formation of the TATA box-bound TBP ternary complex."; /evidence="ECO:0000269|PubMed:29158257"; MUTAGEN 238; /note="K->A: Abolishes autoacetylation, represses transcription activity, does not inhibit its association with chromatin to promoter-specific regions and decreases the association of GTF2F1 with chromatin to promoter-specific regions."; /evidence="ECO:0000269|PubMed:12931194"; MUTAGEN 247; /note="G->V: Inhibits interaction with TBP."; /evidence="ECO:0000269|PubMed:8516312"; MUTAGEN 283; /note="V->A: Reduces DNA-binding."; /evidence="ECO:0000269|PubMed:9420329"; MUTAGEN 286; /note="R->A: Reduces DNA-binding."; /evidence="ECO:0000269|PubMed:9420329"; MUTAGEN 286; /note="R->E: Inhibits interaction with RNA polymerase II; when associated with E-290 and E-295."; /evidence="ECO:0000269|PubMed:8504927"; MUTAGEN 290; /note="R->E: Inhibits interaction with RNA polymerase II; when associated with E-286 and E-295."; /evidence="ECO:0000269|PubMed:8504927"; MUTAGEN 295; /note="R->E: Inhibits interaction with RNA polymerase II; when associated with E-286 and E-290."; /evidence="ECO:0000269|PubMed:8504927
uniprot
proteins
post_translational_modification
PTM: Acetylated (PubMed:24441171). Autoacetylated; autoacetylation at Lys-238 stimulates transcription activation (PubMed:12931194). {ECO:0000269|PubMed:12931194, ECO:0000269|PubMed:24441171}.
uniprot
proteins
protein_family
TFIIB family
uniprot
proteins
pubmed
10318856
uniprot
proteins
pubmed
10359081
uniprot
proteins
pubmed
10619841
uniprot
proteins
pubmed
11005381
uniprot
proteins
pubmed
11045620
uniprot
proteins
pubmed
12931194
uniprot
proteins
pubmed
14641108
uniprot
proteins
pubmed
14702039
uniprot
proteins
pubmed
1517211
uniprot
proteins
pubmed
15489334
uniprot
proteins
pubmed
15654739
uniprot
proteins
pubmed
16230532
uniprot
proteins
pubmed
16710414
uniprot
proteins
pubmed
16959974
uniprot
proteins
pubmed
18669648
uniprot
proteins
pubmed
1876184
uniprot
proteins
pubmed
19054851
uniprot
proteins
pubmed
1946368
uniprot
proteins
pubmed
19690332
uniprot
proteins
pubmed
21269460
uniprot
proteins
pubmed
2247058
uniprot
proteins
pubmed
23186163
uniprot
proteins
pubmed
24441171
uniprot
proteins
pubmed
27193682
uniprot
proteins
pubmed
29158257
uniprot
proteins
pubmed
3029109
uniprot
proteins
pubmed
3818643
uniprot
proteins
pubmed
7601352
uniprot
proteins
pubmed
7671313
uniprot
proteins
pubmed
7675079
uniprot
proteins
pubmed
7983760
uniprot
proteins
pubmed
8392607
uniprot
proteins
pubmed
8413225
uniprot
proteins
pubmed
8504927
uniprot
proteins
pubmed
8515819
uniprot
proteins
pubmed
8515820
uniprot
proteins
pubmed
8516311
uniprot
proteins
pubmed
8516312
uniprot
proteins
pubmed
8566795
uniprot
proteins
pubmed
8662660
uniprot
proteins
pubmed
8800208
uniprot
proteins
pubmed
9420329
uniprot
proteins
pubmed
9609687
uniprot
proteins
sequence_length
316
uniprot
proteins
subcellular_location
SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:12931194}. Chromosome {ECO:0000269|PubMed:24441171}. Note=Non-acetylated form colocalizes with DNA in the G0/1, S and G2 phases of the cell cycle, but not during mitosis (PubMed:24441171). Acetylated form colocalizes at transcriptionally silent mitotic chromatids during mitosis at metaphase, anaphase, and telophase phases of the cell cycle (PubMed:24441171). {ECO:0000269|PubMed:24441171}.
uniprot
proteins