TBP_MOUSE
ID TBP_MOUSE Reviewed; 316 AA.
AC P29037; O09169; Q80UL8; Q8C3S1;
DT 01-DEC-1992, integrated into UniProtKB/Swiss-Prot.
DT 01-DEC-1992, sequence version 1.
DT 03-AUG-2022, entry version 192.
DE RecName: Full=TATA-box-binding protein;
DE AltName: Full=TATA sequence-binding protein;
DE AltName: Full=TATA-binding factor;
DE AltName: Full=TATA-box factor;
DE AltName: Full=Transcription initiation factor TFIID TBP subunit;
GN Name=Tbp; Synonyms=Tfiid;
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 [MRNA].
RX PubMed=1861978; DOI=10.1093/nar/19.14.3861;
RA Tamura T.-A., Sumita K., Fujino I., Aoyama A., Horikoshi M., Hoffmann A.,
RA Roeder R.G., Muramatsu M., Mikoshiba K.;
RT "Striking homology of the 'variable' N-terminal as well as the 'conserved
RT core' domains of the mouse and human TATA-factors (TFIID).";
RL Nucleic Acids Res. 19:3861-3865(1991).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=8332475; DOI=10.1093/nar/21.11.2769;
RA Sumita K., Makino Y., Katoh K., Kashimoto T., Muramatsu M., Mikoshiba K.,
RA Tamura T.-A.;
RT "Structure of a mammalian TBP (TATA-binding protein) gene: isolation of the
RT mouse TBP genome.";
RL Nucleic Acids Res. 21:2769-2769(1993).
RN [3]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC STRAIN=TW18/TW5; TISSUE=Testis;
RX PubMed=9286694; DOI=10.1006/geno.1997.4839;
RA Trachtulec Z., Hamvas R.M., Forejt J., Lehrach H.R., Vincek V., Klein J.;
RT "Linkage of TATA-binding protein and proteasome subunit C5 genes in mice
RT and humans reveals synteny conserved between mammals and invertebrates.";
RL Genomics 44:1-7(1997).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J; TISSUE=Lung;
RX PubMed=16141072; DOI=10.1126/science.1112014;
RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT "The transcriptional landscape of the mammalian genome.";
RL Science 309:1559-1563(2005).
RN [5]
RP TISSUE SPECIFICITY.
RX PubMed=16412700; DOI=10.1016/j.modgep.2005.09.005;
RA Xiao L., Kim M., DeJong J.;
RT "Developmental and cell type-specific regulation of core promoter
RT transcription factors in germ cells of frogs and mice.";
RL Gene Expr. Patterns 6:409-419(2006).
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=B5/EGFP transgenic ICR mice, and FVB/N;
RC TISSUE=Mammary tumor, and Trophoblast;
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 [7]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 1-36.
RX PubMed=8769130; DOI=10.1006/bbrc.1996.1166;
RA Ohbayashi T., Schmidt E.E., Makino Y., Kishimoto T., Nabeshima Y.,
RA Muramatsu M., Tamura T.-A.;
RT "Promoter structure of the mouse TATA-binding protein (TBP) gene.";
RL Biochem. Biophys. Res. Commun. 225:275-280(1996).
RN [8]
RP INTERACTION WITH TAF1A; TAF1B AND TAF1C.
RX PubMed=9050847; DOI=10.1073/pnas.94.5.1733;
RA Heix J., Zomerdijk J.C.B.M., Ravanpay A., Tjian R., Grummt I.;
RT "Cloning of murine RNA polymerase I-specific TAF factors: conserved
RT interactions between the subunits of the species-specific transcription
RT initiation factor TIF-IB/SL1.";
RL Proc. Natl. Acad. Sci. U.S.A. 94:1733-1738(1997).
RN [9]
RP INTERACTION WITH UTF1.
RX PubMed=9524124; DOI=10.1093/emboj/17.7.2019;
RA Okuda A., Fukushima A., Nishimoto M., Orimo A., Yamagishi T., Nabeshima Y.,
RA Kuro-o M., Nabeshima Y., Boon K., Keaveney M., Stunnenberg H.G.,
RA Muramatsu M.;
RT "UTF1, a novel transcriptional coactivator expressed in pluripotent
RT embryonic stem cells and extra-embryonic cells.";
RL EMBO J. 17:2019-2032(1998).
RN [10]
RP INTERACTION WITH CITED2.
RX PubMed=10593900; DOI=10.1074/jbc.274.51.36159;
RA Glenn D.J., Maurer R.A.;
RT "MRG1 binds to the LIM domain of Lhx2 and may function as a coactivator to
RT stimulate glycoprotein hormone alpha-subunit gene expression.";
RL J. Biol. Chem. 274:36159-36167(1999).
RN [11]
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 [12]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Spleen;
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).
RN [13]
RP INTERACTION WITH LLPH.
RX PubMed=26961175; DOI=10.1038/srep22892;
RA Yu N.K., Kim H.F., Shim J., Kim S., Kim D.W., Kwak C., Sim S.E., Choi J.H.,
RA Ahn S., Yoo J., Choi S.L., Jang D.J., Lim C.S., Lee Y.S., Kang C.,
RA Choi S.Y., Kaang B.K.;
RT "A transducible nuclear/nucleolar protein, mLLP, regulates neuronal
RT morphogenesis and synaptic transmission.";
RL Sci. Rep. 6:22892-22892(2016).
CC -!- FUNCTION: General transcription factor that functions at the core of
CC the DNA-binding multiprotein factor TFIID. Binding of TFIID to the TATA
CC box is the initial transcriptional step of the pre-initiation complex
CC (PIC), playing a role in the activation of eukaryotic genes transcribed
CC by RNA polymerase II. Component of a BRF2-containing transcription
CC factor complex that regulates transcription mediated by RNA polymerase
CC III. Component of the transcription factor SL1/TIF-IB complex, which is
CC involved in the assembly of the PIC (pre-initiation complex) during RNA
CC polymerase I-dependent transcription. The rate of PIC formation
CC probably is primarily dependent on the rate of association of SL1 with
CC the rDNA promoter. SL1 is involved in stabilization of nucleolar
CC transcription factor 1/UBTF on rDNA. {ECO:0000250|UniProtKB:P20226}.
CC -!- SUBUNIT: Binds DNA as monomer. Belongs to the TFIID complex together
CC with the TBP-associated factors (TAFs). Part of a TFIID-containing RNA
CC polymerase II pre-initiation complex that is composed of TBP and at
CC least GTF2A1, GTF2A2, GTF2E1, GTF2E2, GTF2F1, GTF2H2, GTF2H3, GTF2H4,
CC GTF2H5, GTF2B, TCEA1, ERCC2, ERCC3, TAF1, TAF2, TAF3, TAF4, TAF5, TAF6,
CC TAF7, TAF8, TAF9, TAF10, TAF11, TAF12 and TAF13 (By similarity).
CC Component of the transcription factor SL1/TIF-IB complex, composed of
CC TBP and at least TAF1A, TAF1B, TAF1C and TAF1D. Association of TBP to
CC form either TFIID or SL1/TIF-IB appears to be mutually exclusive.
CC Interacts with TAF1A, TAF1B and TAF1C (PubMed:9050847). Interacts with
CC TFIIB, NCOA6, DRAP1, DR1 and ELF3. Interacts with SPIB, SNAPC1, SNAPC2
CC and SNAPC4 (By similarity). Interacts with UTF1 (PubMed:9524124).
CC Interacts with BRF2; this interaction promotes recruitment of BRF2 to
CC TATA box-containing promoters. Interacts with UBTF (By similarity).
CC Interacts with GPBP1 (PubMed:14612417). Interacts with CITED2
CC (PubMed:10593900). Interacts with ATF7IP (Probable). Interacts with
CC LLPH (PubMed:26961175). Interacts with HSF1 (via transactivation
CC domain) (By similarity). Interacts with GTF2B (via C-terminus); this
CC interaction with promoter-bound TBP guides RNA polymerase II into the
CC pre-initiation complex (PIC) (By similarity). Interacts with PAX5 (By
CC similarity). {ECO:0000250|UniProtKB:P20226,
CC ECO:0000269|PubMed:10593900, ECO:0000269|PubMed:14612417,
CC ECO:0000269|PubMed:26961175, ECO:0000269|PubMed:9050847,
CC ECO:0000269|PubMed:9524124, ECO:0000305}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:P20226}.
CC -!- TISSUE SPECIFICITY: Ubiquitously expressed.
CC {ECO:0000269|PubMed:16412700}.
CC -!- SIMILARITY: Belongs to the TBP family. {ECO:0000305}.
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DR EMBL; D01034; BAA00840.1; -; mRNA.
DR EMBL; U63933; AAB53097.1; -; mRNA.
DR EMBL; AK085037; BAC39346.1; -; mRNA.
DR EMBL; BC050136; AAH50136.1; -; mRNA.
DR EMBL; BC012685; AAH12685.1; -; mRNA.
DR CCDS; CCDS37454.2; -.
DR PIR; S34437; S34437.
DR RefSeq; NP_038712.3; NM_013684.3.
DR AlphaFoldDB; P29037; -.
DR SMR; P29037; -.
DR BioGRID; 203978; 32.
DR ComplexPortal; CPX-932; General transcription factor complex TFIID.
DR ComplexPortal; CPX-959; General transcription factor complex TFIID, Taf4b variant.
DR CORUM; P29037; -.
DR DIP; DIP-24197N; -.
DR IntAct; P29037; 8.
DR MINT; P29037; -.
DR STRING; 10090.ENSMUSP00000124317; -.
DR iPTMnet; P29037; -.
DR PhosphoSitePlus; P29037; -.
DR EPD; P29037; -.
DR PaxDb; P29037; -.
DR PeptideAtlas; P29037; -.
DR PRIDE; P29037; -.
DR ProteomicsDB; 259361; -.
DR Antibodypedia; 4001; 619 antibodies from 45 providers.
DR DNASU; 21374; -.
DR Ensembl; ENSMUST00000014911; ENSMUSP00000014911; ENSMUSG00000014767.
DR Ensembl; ENSMUST00000117593; ENSMUSP00000112794; ENSMUSG00000014767.
DR Ensembl; ENSMUST00000162505; ENSMUSP00000124317; ENSMUSG00000014767.
DR GeneID; 21374; -.
DR KEGG; mmu:21374; -.
DR UCSC; uc008aon.2; mouse.
DR CTD; 6908; -.
DR MGI; MGI:101838; Tbp.
DR VEuPathDB; HostDB:ENSMUSG00000014767; -.
DR eggNOG; KOG3302; Eukaryota.
DR GeneTree; ENSGT00940000157474; -.
DR HOGENOM; CLU_060161_1_1_1; -.
DR InParanoid; P29037; -.
DR OMA; FGRTNAS; -.
DR OrthoDB; 1219067at2759; -.
DR PhylomeDB; P29037; -.
DR TreeFam; TF300102; -.
DR Reactome; R-MMU-5250924; B-WICH complex positively regulates rRNA expression.
DR Reactome; R-MMU-674695; RNA Polymerase II Pre-transcription Events.
DR Reactome; R-MMU-6804756; Regulation of TP53 Activity through Phosphorylation.
DR Reactome; R-MMU-6807505; RNA polymerase II transcribes snRNA genes.
DR Reactome; R-MMU-73762; RNA Polymerase I Transcription Initiation.
DR Reactome; R-MMU-73772; RNA Polymerase I Promoter Escape.
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-73863; RNA Polymerase I Transcription Termination.
DR Reactome; R-MMU-75953; RNA Polymerase II Transcription Initiation.
DR Reactome; R-MMU-76042; RNA Polymerase II Transcription Initiation And Promoter Clearance.
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 Reactome; R-MMU-76071; RNA Polymerase III Transcription Initiation From Type 3 Promoter.
DR Reactome; R-MMU-9018519; Estrogen-dependent gene expression.
DR BioGRID-ORCS; 21374; 22 hits in 73 CRISPR screens.
DR ChiTaRS; Tbp; mouse.
DR PRO; PR:P29037; -.
DR Proteomes; UP000000589; Chromosome 17.
DR RNAct; P29037; protein.
DR Bgee; ENSMUSG00000014767; Expressed in embryonic post-anal tail and 240 other tissues.
DR ExpressionAtlas; P29037; baseline and differential.
DR Genevisible; P29037; MM.
DR GO; GO:0000785; C:chromatin; ISO:MGI.
DR GO; GO:0005737; C:cytoplasm; IDA:MGI.
DR GO; GO:0000791; C:euchromatin; ISO:MGI.
DR GO; GO:0001674; C:female germ cell nucleus; IDA:MGI.
DR GO; GO:0001939; C:female pronucleus; IDA:MGI.
DR GO; GO:0001673; C:male germ cell nucleus; IDA:MGI.
DR GO; GO:0001940; C:male pronucleus; IDA:MGI.
DR GO; GO:0005654; C:nucleoplasm; ISO:MGI.
DR GO; GO:0005634; C:nucleus; IDA:MGI.
DR GO; GO:0045120; C:pronucleus; IDA:MGI.
DR GO; GO:0032991; C:protein-containing complex; ISO:MGI.
DR GO; GO:0000120; C:RNA polymerase I transcription regulator complex; TAS:MGI.
DR GO; GO:0005668; C:RNA polymerase transcription factor SL1 complex; IPI:MGI.
DR GO; GO:0005672; C:transcription factor TFIIA complex; ISO:MGI.
DR GO; GO:0005669; C:transcription factor TFIID complex; IDA:MGI.
DR GO; GO:0097550; C:transcription preinitiation complex; ISO:MGI.
DR GO; GO:0017162; F:aryl hydrocarbon receptor binding; ISO:MGI.
DR GO; GO:0001046; F:core promoter sequence-specific DNA binding; ISO:MGI.
DR GO; GO:0003677; F:DNA binding; IDA:MGI.
DR GO; GO:0140297; F:DNA-binding transcription factor binding; ISO:MGI.
DR GO; GO:0019899; F:enzyme binding; ISO:MGI.
DR GO; GO:0140223; F:general transcription initiation factor activity; IBA:GO_Central.
DR GO; GO:0000978; F:RNA polymerase II cis-regulatory region sequence-specific DNA binding; IDA:MGI.
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:0001091; F:RNA polymerase II general transcription initiation factor binding; ISO:MGI.
DR GO; GO:0061629; F:RNA polymerase II-specific DNA-binding transcription factor binding; IPI:MGI.
DR GO; GO:0000995; F:RNA polymerase III general transcription initiation factor activity; ISS:UniProtKB.
DR GO; GO:0001093; F:TFIIB-class transcription factor binding; ISO:MGI.
DR GO; GO:0000976; F:transcription cis-regulatory region binding; ISO:MGI.
DR GO; GO:0006352; P:DNA-templated transcription, initiation; IBA:GO_Central.
DR GO; GO:0042789; P:mRNA transcription by RNA polymerase II; ISO:MGI.
DR GO; GO:0060261; P:positive regulation of transcription initiation from RNA polymerase II promoter; ISO:MGI.
DR GO; GO:0045893; P:positive regulation of transcription, DNA-templated; ISO:MGI.
DR GO; GO:0006468; P:protein phosphorylation; ISO:MGI.
DR GO; GO:0051123; P:RNA polymerase II preinitiation complex assembly; ISO:MGI.
DR GO; GO:0006366; P:transcription by RNA polymerase II; IMP:MGI.
DR GO; GO:0006383; P:transcription by RNA polymerase III; IMP:MGI.
DR CDD; cd04516; TBP_eukaryotes; 1.
DR Gene3D; 3.30.310.10; -; 2.
DR HAMAP; MF_00408; TATA_bind_prot_arch; 1.
DR InterPro; IPR000814; TBP.
DR InterPro; IPR030491; TBP_CS.
DR InterPro; IPR012295; TBP_dom_sf.
DR InterPro; IPR033710; TBP_eukaryotic.
DR PANTHER; PTHR10126; PTHR10126; 1.
DR Pfam; PF00352; TBP; 2.
DR PRINTS; PR00686; TIFACTORIID.
DR PROSITE; PS00351; TFIID; 2.
PE 1: Evidence at protein level;
KW DNA-binding; Nucleus; Reference proteome; Repeat; Transcription;
KW Transcription regulation.
FT CHAIN 1..316
FT /note="TATA-box-binding protein"
FT /id="PRO_0000153958"
FT REPEAT 142..218
FT /note="1"
FT REPEAT 232..309
FT /note="2"
FT REGION 1..21
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 104..135
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 112..126
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT VARIANT 70
FT /note="Q -> QQQ (in strain: TW18/TW5)"
FT CONFLICT 141
FT /note="Q -> R (in Ref. 6; AAH50136)"
FT /evidence="ECO:0000305"
FT CONFLICT 164
FT /note="A -> P (in Ref. 4; BAC39346)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 316 AA; 34709 MW; A33D776160B4A393 CRC64;
MDQNNSLPPY AQGLASPQGA MTPGIPIFSP MMPYGTGLTP QPIQNTNSLS ILEEQQRQQQ
QQQQQQQQQQ AVATAAASVQ QSTSQQPTQG ASGQTPQLFH SQTLTTAPLP GTTPLYPSPM
TPMTPITPAT PASESSGIVP QLQNIVSTVN LGCKLDLKTI ALRARNAEYN PKRFAAVIMR
IREPRTTALI FSSGKMVCTG AKSEEQSRLA ARKYARVVQK LGFPAKFLDF KIQNMVGSCD
VKFPIRLEGL VLTHQQFSSY EPELFPGLIY RMIKPRIVLL IFVSGKVVLT GAKVRAEIYE
AFENIYPILK GFRKTT
