ID B1APE2_HUMAN Unreviewed; 231 AA. AC B1APE2; DT 08-APR-2008, integrated into UniProtKB/TrEMBL. DT 08-APR-2008, sequence version 1. DT 27-NOV-2024, entry version 123. DE RecName: Full=Transcription initiation factor IIB {ECO:0000256|ARBA:ARBA00013932}; DE EC=2.3.1.48 {ECO:0000256|ARBA:ARBA00013184}; DE AltName: Full=General transcription factor TFIIB {ECO:0000256|ARBA:ARBA00031706}; DE Flags: Fragment; GN Name=GTF2B {ECO:0000313|Ensembl:ENSP00000402345.1}; OS Homo sapiens (Human). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia; OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae; OC Homo. OX NCBI_TaxID=9606 {ECO:0000313|Ensembl:ENSP00000402345.1, ECO:0000313|Proteomes:UP000005640}; RN [1] {ECO:0000313|Ensembl:ENSP00000402345.1} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RX PubMed=11237011; DOI=10.1038/35057062; RG International Human Genome Sequencing Consortium; RA Lander E.S., Linton L.M., Birren B., Nusbaum C., Zody M.C., Baldwin J., RA Devon K., Dewar K., Doyle M., FitzHugh W., Funke R., Gage D., Harris K., RA Heaford A., Howland J., Kann L., Lehoczky J., LeVine R., McEwan P., RA McKernan K., Meldrim J., Mesirov J.P., Miranda C., Morris W., Naylor J., RA Raymond C., Rosetti M., Santos R., Sheridan A., Sougnez C., RA Stange-Thomann N., Stojanovic N., Subramanian A., Wyman D., Rogers J., RA Sulston J., Ainscough R., Beck S., Bentley D., Burton J., Clee C., RA Carter N., Coulson A., Deadman R., Deloukas P., Dunham A., Dunham I., RA Durbin R., French L., Grafham D., Gregory S., Hubbard T., Humphray S., RA Hunt A., Jones M., Lloyd C., McMurray A., Matthews L., Mercer S., Milne S., RA Mullikin J.C., Mungall A., Plumb R., Ross M., Shownkeen R., Sims S., RA Waterston R.H., Wilson R.K., Hillier L.W., McPherson J.D., Marra M.A., RA Mardis E.R., Fulton L.A., Chinwalla A.T., Pepin K.H., Gish W.R., RA Chissoe S.L., Wendl M.C., Delehaunty K.D., Miner T.L., Delehaunty A., RA Kramer J.B., Cook L.L., Fulton R.S., Johnson D.L., Minx P.J., Clifton S.W., RA Hawkins T., Branscomb E., Predki P., Richardson P., Wenning S., Slezak T., RA Doggett N., Cheng J.F., Olsen A., Lucas S., Elkin C., Uberbacher E., RA Frazier M., Gibbs R.A., Muzny D.M., Scherer S.E., Bouck J.B., RA Sodergren E.J., Worley K.C., Rives C.M., Gorrell J.H., Metzker M.L., RA Naylor S.L., Kucherlapati R.S., Nelson D.L., Weinstock G.M., Sakaki Y., RA Fujiyama A., Hattori M., Yada T., Toyoda A., Itoh T., Kawagoe C., RA Watanabe H., Totoki Y., Taylor T., Weissenbach J., Heilig R., Saurin W., RA Artiguenave F., Brottier P., Bruls T., Pelletier E., Robert C., Wincker P., RA Smith D.R., Doucette-Stamm L., Rubenfield M., Weinstock K., Lee H.M., RA Dubois J., Rosenthal A., Platzer M., Nyakatura G., Taudien S., Rump A., RA Yang H., Yu J., Wang J., Huang G., Gu J., Hood L., Rowen L., Madan A., RA Qin S., Davis R.W., Federspiel N.A., Abola A.P., Proctor M.J., Myers R.M., RA Schmutz J., Dickson M., Grimwood J., Cox D.R., Olson M.V., Kaul R., RA Raymond C., Shimizu N., Kawasaki K., Minoshima S., Evans G.A., RA Athanasiou M., Schultz R., Roe B.A., Chen F., Pan H., Ramser J., RA Lehrach H., Reinhardt R., McCombie W.R., de la Bastide M., Dedhia N., RA Blocker H., Hornischer K., Nordsiek G., Agarwala R., Aravind L., RA Bailey J.A., Bateman A., Batzoglou S., Birney E., Bork P., Brown D.G., RA Burge C.B., Cerutti L., Chen H.C., Church D., Clamp M., Copley R.R., RA Doerks T., Eddy S.R., Eichler E.E., Furey T.S., Galagan J., Gilbert J.G., RA Harmon C., Hayashizaki Y., Haussler D., Hermjakob H., Hokamp K., Jang W., RA Johnson L.S., Jones T.A., Kasif S., Kaspryzk A., Kennedy S., Kent W.J., RA Kitts P., Koonin E.V., Korf I., Kulp D., Lancet D., Lowe T.M., RA McLysaght A., Mikkelsen T., Moran J.V., Mulder N., Pollara V.J., RA Ponting C.P., Schuler G., Schultz J., Slater G., Smit A.F., Stupka E., RA Szustakowski J., Thierry-Mieg D., Thierry-Mieg J., Wagner L., Wallis J., RA Wheeler R., Williams A., Wolf Y.I., Wolfe K.H., Yang S.P., Yeh R.F., RA Collins F., Guyer M.S., Peterson J., Felsenfeld A., Wetterstrand K.A., RA Patrinos A., Morgan M.J., de Jong P., Catanese J.J., Osoegawa K., RA Shizuya H., Choi S., Chen Y.J.; RT "Initial sequencing and analysis of the human genome."; RL Nature 409:860-921(2001). RN [2] {ECO:0000313|Ensembl:ENSP00000402345.1} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RX PubMed=15496913; DOI=10.1038/nature03001; RG International Human Genome Sequencing Consortium; RT "Finishing the euchromatic sequence of the human genome."; RL Nature 431:931-945(2004). RN [3] {ECO:0000313|Ensembl:ENSP00000402345.1, ECO:0000313|Proteomes:UP000005640} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RX PubMed=16710414; DOI=10.1038/nature04727; RA Gregory S.G., Barlow K.F., McLay K.E., Kaul R., Swarbreck D., Dunham A., RA Scott C.E., Howe K.L., Woodfine K., Spencer C.C., Jones M.C., Gillson C., RA Searle S., Zhou Y., Kokocinski F., McDonald L., Evans R., Phillips K., RA Atkinson A., Cooper R., Jones C., Hall R.E., Andrews T.D., Lloyd C., RA Ainscough R., Almeida J.P., Ambrose K.D., Anderson F., Andrew R.W., RA Ashwell R.I., Aubin K., Babbage A.K., Bagguley C.L., Bailey J., Beasley H., RA Bethel G., Bird C.P., Bray-Allen S., Brown J.Y., Brown A.J., Buckley D., RA Burton J., Bye J., Carder C., Chapman J.C., Clark S.Y., Clarke G., Clee C., RA Cobley V., Collier R.E., Corby N., Coville G.J., Davies J., Deadman R., RA Dunn M., Earthrowl M., Ellington A.G., Errington H., Frankish A., RA Frankland J., French L., Garner P., Garnett J., Gay L., Ghori M.R., RA Gibson R., Gilby L.M., Gillett W., Glithero R.J., Grafham D.V., RA Griffiths C., Griffiths-Jones S., Grocock R., Hammond S., Harrison E.S., RA Hart E., Haugen E., Heath P.D., Holmes S., Holt K., Howden P.J., Hunt A.R., RA Hunt S.E., Hunter G., Isherwood J., James R., Johnson C., Johnson D., RA Joy A., Kay M., Kershaw J.K., Kibukawa M., Kimberley A.M., King A., RA Knights A.J., Lad H., Laird G., Lawlor S., Leongamornlert D.A., Lloyd D.M., RA Loveland J., Lovell J., Lush M.J., Lyne R., Martin S., RA Mashreghi-Mohammadi M., Matthews L., Matthews N.S., McLaren S., Milne S., RA Mistry S., Moore M.J., Nickerson T., O'Dell C.N., Oliver K., Palmeiri A., RA Palmer S.A., Parker A., Patel D., Pearce A.V., Peck A.I., Pelan S., RA Phelps K., Phillimore B.J., Plumb R., Rajan J., Raymond C., Rouse G., RA Saenphimmachak C., Sehra H.K., Sheridan E., Shownkeen R., Sims S., RA Skuce C.D., Smith M., Steward C., Subramanian S., Sycamore N., Tracey A., RA Tromans A., Van Helmond Z., Wall M., Wallis J.M., White S., Whitehead S.L., RA Wilkinson J.E., Willey D.L., Williams H., Wilming L., Wray P.W., Wu Z., RA Coulson A., Vaudin M., Sulston J.E., Durbin R., Hubbard T., Wooster R., RA Dunham I., Carter N.P., McVean G., Ross M.T., Harrow J., Olson M.V., RA Beck S., Rogers J., Bentley D.R., Banerjee R., Bryant S.P., Burford D.C., RA Burrill W.D., Clegg S.M., Dhami P., Dovey O., Faulkner L.M., Gribble S.M., RA Langford C.F., Pandian R.D., Porter K.M., Prigmore E.; RT "The DNA sequence and biological annotation of human chromosome 1."; RL Nature 441:315-321(2006). RN [4] {ECO:0007829|PubMed:18669648} RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RX PubMed=18669648; DOI=10.1073/pnas.0805139105; RA Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E., RA Elledge S.J., Gygi S.P.; RT "A quantitative atlas of mitotic phosphorylation."; RL Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008). RN [5] {ECO:0007829|PubMed:19690332} RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RX PubMed=19690332; DOI=10.1126/scisignal.2000007; RA Mayya V., Lundgren D.H., Hwang S.I., Rezaul K., Wu L., Eng J.K., RA Rodionov V., Han D.K.; RT "Quantitative phosphoproteomic analysis of T cell receptor signaling RT reveals system-wide modulation of protein-protein interactions."; RL Sci. Signal. 2:RA46-RA46(2009). RN [6] {ECO:0007829|PubMed:21269460} RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RX PubMed=21269460; DOI=10.1186/1752-0509-5-17; RA Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Burckstummer T., RA Bennett K.L., Superti-Furga G., Colinge J.; RT "Initial characterization of the human central proteome."; RL BMC Syst. Biol. 5:17-17(2011). RN [7] {ECO:0007829|PubMed:23186163} RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RX PubMed=23186163; RA Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J., RA Mohammed S.; RT "Toward a comprehensive characterization of a human cancer cell RT phosphoproteome."; RL J. Proteome Res. 12:260-271(2013). RN [8] {ECO:0000313|Ensembl:ENSP00000402345.1} RP IDENTIFICATION. RG Ensembl; RL Submitted (AUG-2024) to UniProtKB. 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:0000256|ARBA:ARBA00045843}. CC -!- CATALYTIC ACTIVITY: CC Reaction=L-lysyl-[protein] + acetyl-CoA = N(6)-acetyl-L-lysyl-[protein] CC + CoA + H(+); Xref=Rhea:RHEA:45948, Rhea:RHEA-COMP:9752, Rhea:RHEA- CC COMP:10731, ChEBI:CHEBI:15378, ChEBI:CHEBI:29969, ChEBI:CHEBI:57287, CC ChEBI:CHEBI:57288, ChEBI:CHEBI:61930; EC=2.3.1.48; CC Evidence={ECO:0000256|ARBA:ARBA00000780}; CC -!- SIMILARITY: Belongs to the TFIIB family. CC {ECO:0000256|ARBA:ARBA00010857}. 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; AL445991; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR AlphaFoldDB; B1APE2; -. DR SMR; B1APE2; -. DR MassIVE; B1APE2; -. DR PeptideAtlas; B1APE2; -. DR Antibodypedia; 19819; 469 antibodies from 36 providers. DR Ensembl; ENST00000418217.1; ENSP00000402345.1; ENSG00000137947.12. DR UCSC; uc057idc.1; human. DR HGNC; HGNC:4648; GTF2B. DR VEuPathDB; HostDB:ENSG00000137947; -. DR GeneTree; ENSGT00390000006671; -. DR HOGENOM; CLU_043736_1_1_1; -. DR ChiTaRS; GTF2B; human. DR Proteomes; UP000005640; Chromosome 1. DR Bgee; ENSG00000137947; Expressed in oocyte and 204 other cell types or tissues. DR ExpressionAtlas; B1APE2; baseline and differential. DR GO; GO:0016604; C:nuclear body; IDA:HPA. DR GO; GO:0005654; C:nucleoplasm; IDA:HPA. DR GO; GO:0004402; F:histone acetyltransferase activity; IEA:UniProtKB-EC. DR GO; GO:0017025; F:TBP-class protein binding; IEA:InterPro. DR GO; GO:0070897; P:transcription preinitiation complex assembly; IEA:InterPro. DR CDD; cd20551; CYCLIN_TFIIB_rpt1; 1. DR FunFam; 1.10.472.10:FF:000019; transcription initiation factor IIB; 1. DR Gene3D; 2.20.25.10; -; 1. DR Gene3D; 1.10.472.10; Cyclin-like; 1. 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; 1. DR PRINTS; PR00685; TIFACTORIIB. DR SMART; SM00385; CYCLIN; 1. DR SUPFAM; SSF47954; Cyclin-like; 1. DR SUPFAM; SSF57783; Zinc beta-ribbon; 1. DR PROSITE; PS00782; TFIIB; 1. DR PROSITE; PS51134; ZF_TFIIB; 1. PE 1: Evidence at protein level; KW Metal-binding {ECO:0000256|PROSITE-ProRule:PRU00469}; KW Proteomics identification {ECO:0007829|PeptideAtlas:B1APE2, KW ECO:0007829|ProteomicsDB:B1APE2}; KW Reference proteome {ECO:0000313|Proteomes:UP000005640}; KW Repeat {ECO:0000256|ARBA:ARBA00022737}; KW Transcription {ECO:0000256|ARBA:ARBA00023163}; KW Transcription regulation {ECO:0000256|ARBA:ARBA00023015}; KW Zinc {ECO:0000256|PROSITE-ProRule:PRU00469}; KW Zinc-finger {ECO:0000256|PROSITE-ProRule:PRU00469}. FT DOMAIN 11..42 FT /note="TFIIB-type" FT /evidence="ECO:0000259|PROSITE:PS51134" FT REGION 51..70 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT NON_TER 231 FT /evidence="ECO:0000313|Ensembl:ENSP00000402345.1" SQ SEQUENCE 231 AA; 25636 MW; 080BAE8E0C28DD97 CRC64; MASTSRLDAL PRVTCPNHPD AILVEDYRAG DMICPECDRV IDVGSEWRTF SNDKATKDPS RVGDSQNPLL SDGDLSTMIG KGTGAASFDE FGNSKYQNRR TMSSSDRAMM NAFKEITTMA DRINLPRNIV DRTNNLFKQV YEQKSLKGRA NDAIASACLY IACRQEGVPR TFKEICAVSR ISKKEIGRCF KLILKALETS VDLITTGDFM SRFCSNLCLP KQVQMAATHI A //