TBP1_ARATH
ID TBP1_ARATH Reviewed; 200 AA.
AC P28147; Q53YT8;
DT 01-DEC-1992, integrated into UniProtKB/Swiss-Prot.
DT 01-DEC-1992, sequence version 1.
DT 03-AUG-2022, entry version 172.
DE RecName: Full=TATA-box-binding protein 1 {ECO:0000303|PubMed:19929880};
DE Short=AtTBP1 {ECO:0000303|PubMed:19929880};
DE AltName: Full=TATA sequence-binding protein 1 {ECO:0000303|PubMed:19929880};
DE Short=TBP-1 {ECO:0000303|PubMed:19929880};
DE AltName: Full=TATA-binding factor 1 {ECO:0000303|PubMed:19929880};
DE AltName: Full=TATA-box factor 1 {ECO:0000303|PubMed:19929880};
DE AltName: Full=Transcription initiation factor TFIID TBP-1 subunit {ECO:0000303|PubMed:2197561};
GN Name=TBP1 {ECO:0000303|PubMed:19929880};
GN OrderedLocusNames=At3g13445 {ECO:0000312|Araport:AT3G13445};
GN ORFNames=MRP15.10 {ECO:0000312|EMBL:BAB01751.1};
OS Arabidopsis thaliana (Mouse-ear cress).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC rosids; malvids; Brassicales; Brassicaceae; Camelineae; Arabidopsis.
OX NCBI_TaxID=3702;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], AND FUNCTION.
RX PubMed=2197561; DOI=10.1038/346390a0;
RA Gasch A., Hoffmann A., Horikoshi M., Roeder R.G., Chua N.-H.;
RT "Arabidopsis thaliana contains two genes for TFIID.";
RL Nature 346:390-394(1990).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA].
RA Lawit S.J., Gurley W.B.;
RT "Binary protein-protein interactions of the Arabidopsis thaliana general
RT transcription factor IId.";
RL Submitted (NOV-2003) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Columbia;
RX PubMed=10907853; DOI=10.1093/dnares/7.3.217;
RA Kaneko T., Katoh T., Sato S., Nakamura Y., Asamizu E., Tabata S.;
RT "Structural analysis of Arabidopsis thaliana chromosome 3. II. Sequence
RT features of the 4,251,695 bp regions covered by 90 P1, TAC and BAC
RT clones.";
RL DNA Res. 7:217-221(2000).
RN [4]
RP GENOME REANNOTATION.
RC STRAIN=cv. Columbia;
RX PubMed=27862469; DOI=10.1111/tpj.13415;
RA Cheng C.Y., Krishnakumar V., Chan A.P., Thibaud-Nissen F., Schobel S.,
RA Town C.D.;
RT "Araport11: a complete reannotation of the Arabidopsis thaliana reference
RT genome.";
RL Plant J. 89:789-804(2017).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=cv. Columbia;
RX PubMed=14593172; DOI=10.1126/science.1088305;
RA Yamada K., Lim J., Dale J.M., Chen H., Shinn P., Palm C.J., Southwick A.M.,
RA Wu H.C., Kim C.J., Nguyen M., Pham P.K., Cheuk R.F., Karlin-Newmann G.,
RA Liu S.X., Lam B., Sakano H., Wu T., Yu G., Miranda M., Quach H.L.,
RA Tripp M., Chang C.H., Lee J.M., Toriumi M.J., Chan M.M., Tang C.C.,
RA Onodera C.S., Deng J.M., Akiyama K., Ansari Y., Arakawa T., Banh J.,
RA Banno F., Bowser L., Brooks S.Y., Carninci P., Chao Q., Choy N., Enju A.,
RA Goldsmith A.D., Gurjal M., Hansen N.F., Hayashizaki Y., Johnson-Hopson C.,
RA Hsuan V.W., Iida K., Karnes M., Khan S., Koesema E., Ishida J., Jiang P.X.,
RA Jones T., Kawai J., Kamiya A., Meyers C., Nakajima M., Narusaka M.,
RA Seki M., Sakurai T., Satou M., Tamse R., Vaysberg M., Wallender E.K.,
RA Wong C., Yamamura Y., Yuan S., Shinozaki K., Davis R.W., Theologis A.,
RA Ecker J.R.;
RT "Empirical analysis of transcriptional activity in the Arabidopsis
RT genome.";
RL Science 302:842-846(2003).
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RA Brover V.V., Troukhan M.E., Alexandrov N.A., Lu Y.-P., Flavell R.B.,
RA Feldmann K.A.;
RT "Full-length cDNA from Arabidopsis thaliana.";
RL Submitted (MAR-2002) to the EMBL/GenBank/DDBJ databases.
RN [7]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RA Fujita M., Mizukado S., Seki M., Shinozaki K., Mitsuda N., Takiguchi Y.,
RA Takagi M.;
RT "ORF cloning and analysis of Arabidopsis transcription factor genes.";
RL Submitted (MAR-2009) to the EMBL/GenBank/DDBJ databases.
RN [8]
RP INTERACTION WITH TAF1.
RX PubMed=17340043; DOI=10.1007/s11103-007-9135-1;
RA Lawit S.J., O'Grady K., Gurley W.B., Czarnecka-Verner E.;
RT "Yeast two-hybrid map of Arabidopsis TFIID.";
RL Plant Mol. Biol. 64:73-87(2007).
RN [9]
RP INTERACTION WITH PWP2, AND SUBCELLULAR LOCATION.
RC STRAIN=cv. Columbia;
RX PubMed=19929880; DOI=10.1111/j.1365-313x.2009.04081.x;
RA Matsui K., Ohme-Takagi M.;
RT "Detection of protein-protein interactions in plants using the
RT transrepressive activity of the EAR motif repression domain.";
RL Plant J. 61:570-578(2010).
RN [10]
RP SUBUNIT.
RC STRAIN=cv. Wassilewskija;
RX PubMed=21266657; DOI=10.1105/tpc.110.080150;
RA Ding Y., Avramova Z., Fromm M.;
RT "Two distinct roles of ARABIDOPSIS HOMOLOG OF TRITHORAX1 (ATX1) at
RT promoters and within transcribed regions of ATX1-regulated genes.";
RL Plant Cell 23:350-363(2011).
RN [11]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT THR-2, CLEAVAGE OF INITIATOR
RP METHIONINE [LARGE SCALE ANALYSIS], AND IDENTIFICATION BY MASS SPECTROMETRY
RP [LARGE SCALE ANALYSIS].
RX PubMed=22223895; DOI=10.1074/mcp.m111.015131;
RA Bienvenut W.V., Sumpton D., Martinez A., Lilla S., Espagne C., Meinnel T.,
RA Giglione C.;
RT "Comparative large-scale characterisation of plant vs. mammal proteins
RT reveals similar and idiosyncratic N-alpha acetylation features.";
RL Mol. Cell. Proteomics 11:M111.015131-M111.015131(2012).
RN [12]
RP INTERACTION WITH MEE12/CCG1.
RX PubMed=26462908; DOI=10.1105/tpc.15.00370;
RA Li H.J., Zhu S.S., Zhang M.X., Wang T., Liang L., Xue Y., Shi D.Q., Liu J.,
RA Yang W.C.;
RT "Arabidopsis CBP1 is a novel regulator of transcription initiation in
RT central cell-mediated pollen tube guidance.";
RL Plant Cell 27:2880-2893(2015).
RN [13]
RP X-RAY CRYSTALLOGRAPHY (2.1 ANGSTROMS) OF 7-199.
RX PubMed=7634102; DOI=10.1038/nsb0994-621;
RA Nikolov D.B., Burley S.K.;
RT "2.1 A resolution refined structure of a TATA box-binding protein (TBP).";
RL Nat. Struct. Biol. 1:621-637(1994).
RN [14]
RP X-RAY CRYSTALLOGRAPHY (2.7 ANGSTROMS) OF COMPLEX WITH TFIIB.
RX PubMed=7675079; DOI=10.1038/377119a0;
RA Nikolov D.B., Chen H., Halay E.D., Usheva A.A., Hisatake K., Lee D.K.,
RA Roeder R.G., Burley S.K.;
RT "Crystal structure of a TFIIB-TBP-TATA-element ternary complex.";
RL Nature 377:119-128(1995).
RN [15]
RP X-RAY CRYSTALLOGRAPHY (1.9 ANGSTROMS).
RX PubMed=10617571; DOI=10.1101/gad.13.24.3217;
RA Patikoglou G.A., Kim J.L., Sun L., Yang S.H., Kodadek T., Burley S.K.;
RT "TATA element recognition by the TATA box-binding protein has been
RT conserved throughout evolution.";
RL Genes Dev. 13:3217-3230(1999).
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. {ECO:0000269|PubMed:2197561}.
CC -!- SUBUNIT: Belongs to the TFIID complex together with the TBP-associated
CC factors (TAFs) (PubMed:7675079). Binds DNA as monomer. Interacts with
CC TAF1 (via N-terminus) (PubMed:17340043). Interacts with MEE12/CCG1
CC (PubMed:26462908). Associates with PWP2 in the nucleus
CC (PubMed:19929880). Component of a nuclear protein complex containing at
CC least TATA binding proteins (TBPs, e.g. TBP1 and TBP2) and ATX1
CC (PubMed:21266657). {ECO:0000269|PubMed:17340043,
CC ECO:0000269|PubMed:19929880, ECO:0000269|PubMed:21266657,
CC ECO:0000269|PubMed:26462908, ECO:0000269|PubMed:7675079}.
CC -!- INTERACTION:
CC P28147; P41151: HSFA1A; NbExp=3; IntAct=EBI-1247453, EBI-1544927;
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:19929880}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=1;
CC Comment=A number of isoforms are produced. According to EST
CC sequences. {ECO:0000312|Araport:AT3G13445};
CC Name=1;
CC IsoId=P28147-1; Sequence=Displayed;
CC -!- SIMILARITY: Belongs to the TBP family. {ECO:0000305}.
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DR EMBL; X54996; CAA38743.1; -; mRNA.
DR EMBL; AY463625; AAR28027.1; -; mRNA.
DR EMBL; AP000603; BAB01751.1; -; Genomic_DNA.
DR EMBL; CP002686; AEE75355.1; -; Genomic_DNA.
DR EMBL; AF324696; AAG40047.1; -; mRNA.
DR EMBL; AF327429; AAG42019.1; -; mRNA.
DR EMBL; AF349523; AAK15570.1; -; mRNA.
DR EMBL; AY054608; AAK96799.1; -; mRNA.
DR EMBL; AY072455; AAL66870.1; -; mRNA.
DR EMBL; AY084881; AAM61444.1; -; mRNA.
DR EMBL; AB493611; BAH30449.1; -; mRNA.
DR PIR; S10946; S10946.
DR RefSeq; NP_187953.1; NM_112190.5. [P28147-1]
DR PDB; 1QN3; X-ray; 1.95 A; A/B=1-200.
DR PDB; 1QN4; X-ray; 1.86 A; A/B=1-200.
DR PDB; 1QN5; X-ray; 1.93 A; A/B=1-200.
DR PDB; 1QN6; X-ray; 2.10 A; A/B=1-200.
DR PDB; 1QN7; X-ray; 2.30 A; A/B=1-200.
DR PDB; 1QN8; X-ray; 2.10 A; A/B=1-200.
DR PDB; 1QN9; X-ray; 1.90 A; A/B=1-200.
DR PDB; 1QNA; X-ray; 1.80 A; A/B=1-200.
DR PDB; 1QNB; X-ray; 2.23 A; A/B=1-200.
DR PDB; 1QNC; X-ray; 2.30 A; A/B=1-200.
DR PDB; 1QNE; X-ray; 1.90 A; A/B=1-200.
DR PDB; 1VOK; X-ray; 2.10 A; A/B=1-200.
DR PDB; 1VOL; X-ray; 2.70 A; B=1-200.
DR PDB; 1VTL; X-ray; 2.25 A; E/F=13-198.
DR PDB; 1VTO; X-ray; 1.90 A; A/B=11-200.
DR PDB; 6NJQ; X-ray; 2.75 A; A/B=1-200.
DR PDB; 6UEO; X-ray; 2.00 A; A/D/G/J=1-200.
DR PDB; 6UEP; X-ray; 2.05 A; A/B=1-200.
DR PDB; 6UEQ; X-ray; 2.40 A; B=1-200.
DR PDB; 6UER; X-ray; 2.50 A; A/B=1-200.
DR PDBsum; 1QN3; -.
DR PDBsum; 1QN4; -.
DR PDBsum; 1QN5; -.
DR PDBsum; 1QN6; -.
DR PDBsum; 1QN7; -.
DR PDBsum; 1QN8; -.
DR PDBsum; 1QN9; -.
DR PDBsum; 1QNA; -.
DR PDBsum; 1QNB; -.
DR PDBsum; 1QNC; -.
DR PDBsum; 1QNE; -.
DR PDBsum; 1VOK; -.
DR PDBsum; 1VOL; -.
DR PDBsum; 1VTL; -.
DR PDBsum; 1VTO; -.
DR PDBsum; 6NJQ; -.
DR PDBsum; 6UEO; -.
DR PDBsum; 6UEP; -.
DR PDBsum; 6UEQ; -.
DR PDBsum; 6UER; -.
DR AlphaFoldDB; P28147; -.
DR SMR; P28147; -.
DR BioGRID; 5880; 2.
DR IntAct; P28147; 3.
DR MINT; P28147; -.
DR STRING; 3702.AT3G13445.1; -.
DR iPTMnet; P28147; -.
DR PaxDb; P28147; -.
DR PRIDE; P28147; -.
DR ProteomicsDB; 234157; -. [P28147-1]
DR EnsemblPlants; AT3G13445.1; AT3G13445.1; AT3G13445. [P28147-1]
DR GeneID; 820546; -.
DR Gramene; AT3G13445.1; AT3G13445.1; AT3G13445. [P28147-1]
DR KEGG; ath:AT3G13445; -.
DR Araport; AT3G13445; -.
DR TAIR; locus:2092905; AT3G13445.
DR eggNOG; KOG3302; Eukaryota.
DR HOGENOM; CLU_060161_4_2_1; -.
DR InParanoid; P28147; -.
DR OMA; ITGCEVR; -.
DR OrthoDB; 1219067at2759; -.
DR PhylomeDB; P28147; -.
DR EvolutionaryTrace; P28147; -.
DR PRO; PR:P28147; -.
DR Proteomes; UP000006548; Chromosome 3.
DR ExpressionAtlas; P28147; baseline and differential.
DR Genevisible; P28147; AT.
DR GO; GO:0005634; C:nucleus; IDA:UniProtKB.
DR GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
DR GO; GO:0140223; F:general transcription initiation factor activity; IBA:GO_Central.
DR GO; GO:0016251; F:RNA polymerase II general transcription initiation factor activity; IBA:GO_Central.
DR GO; GO:0006352; P:DNA-templated transcription, initiation; IBA:GO_Central.
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 3D-structure; Acetylation; Activator; Alternative splicing; DNA-binding;
KW Nucleus; Reference proteome; Repeat; Transcription;
KW Transcription regulation.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0007744|PubMed:22223895"
FT CHAIN 2..200
FT /note="TATA-box-binding protein 1"
FT /id="PRO_0000153976"
FT REPEAT 25..101
FT /note="1"
FT /evidence="ECO:0000255"
FT REPEAT 115..192
FT /note="2"
FT /evidence="ECO:0000255"
FT MOD_RES 2
FT /note="N-acetylthreonine"
FT /evidence="ECO:0007744|PubMed:22223895"
FT TURN 14..16
FT /evidence="ECO:0007829|PDB:1QNA"
FT STRAND 24..33
FT /evidence="ECO:0007829|PDB:1QNA"
FT HELIX 40..46
FT /evidence="ECO:0007829|PDB:1QNA"
FT STRAND 48..52
FT /evidence="ECO:0007829|PDB:1QNA"
FT TURN 54..56
FT /evidence="ECO:0007829|PDB:1QNA"
FT STRAND 58..64
FT /evidence="ECO:0007829|PDB:1QNA"
FT TURN 65..68
FT /evidence="ECO:0007829|PDB:1QNA"
FT STRAND 69..73
FT /evidence="ECO:0007829|PDB:1QNA"
FT STRAND 77..86
FT /evidence="ECO:0007829|PDB:1QNA"
FT HELIX 87..103
FT /evidence="ECO:0007829|PDB:1QNA"
FT STRAND 111..123
FT /evidence="ECO:0007829|PDB:1QNA"
FT HELIX 130..136
FT /evidence="ECO:0007829|PDB:1QNA"
FT TURN 137..140
FT /evidence="ECO:0007829|PDB:1QNA"
FT STRAND 141..143
FT /evidence="ECO:0007829|PDB:1VOK"
FT TURN 145..147
FT /evidence="ECO:0007829|PDB:1QNA"
FT STRAND 149..155
FT /evidence="ECO:0007829|PDB:1QNA"
FT TURN 156..159
FT /evidence="ECO:0007829|PDB:1QNA"
FT STRAND 160..164
FT /evidence="ECO:0007829|PDB:1QNA"
FT STRAND 168..177
FT /evidence="ECO:0007829|PDB:1QNA"
FT HELIX 178..194
FT /evidence="ECO:0007829|PDB:1QNA"
SQ SEQUENCE 200 AA; 22368 MW; 9E15DC2308818919 CRC64;
MTDQGLEGSN PVDLSKHPSG IVPTLQNIVS TVNLDCKLDL KAIALQARNA EYNPKRFAAV
IMRIREPKTT ALIFASGKMV CTGAKSEDFS KMAARKYARI VQKLGFPAKF KDFKIQNIVG
SCDVKFPIRL EGLAYSHAAF SSYEPELFPG LIYRMKVPKI VLLIFVSGKI VITGAKMRDE
TYKAFENIYP VLSEFRKIQQ
