ID TBP1_ARATH Reviewed; 200 AA. AC P28147; DT 01-DEC-1992, integrated into UniProtKB/Swiss-Prot. DT 01-DEC-1992, sequence version 1. DT 25-NOV-2008, entry version 70. DE RecName: Full=TATA-box-binding protein 1; DE AltName: Full=TATA-box factor 1; DE AltName: Full=TATA-binding factor 1; DE AltName: Full=TATA sequence-binding protein 1; DE Short=TBP-1; DE AltName: Full=Transcription initiation factor TFIID TBP-1 subunit; GN Name=TBP1; OrderedLocusNames=At3g13445; ORFNames=MRP15.10; OS Arabidopsis thaliana (Mouse-ear cress). OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta; OC Spermatophyta; Magnoliophyta; eudicotyledons; core eudicotyledons; OC rosids; eurosids II; Brassicales; Brassicaceae; Arabidopsis. OX NCBI_TaxID=3702; RN [1] RP NUCLEOTIDE SEQUENCE. RX MEDLINE=90326196; 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 [LARGE SCALE GENOMIC DNA]. RC STRAIN=cv. Columbia; RX MEDLINE=20363099; 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. RT Sequence features of the 4,251,695 bp regions covered by 90 P1, TAC RT and BAC clones."; RL DNA Res. 7:217-221(2000). RN [3] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. RC STRAIN=cv. Columbia; RX MEDLINE=22954850; PubMed=14593172; DOI=10.1126/science.1088305; RA Yamada K., Lim J., Dale J.M., Chen H., Shinn P., Palm C.J., RA Southwick A.M., Wu H.C., Kim C.J., Nguyen M., Pham P.K., Cheuk R.F., RA Karlin-Newmann G., Liu S.X., Lam B., Sakano H., Wu T., Yu G., RA Miranda M., Quach H.L., Tripp M., Chang C.H., Lee J.M., Toriumi M.J., RA Chan M.M., Tang C.C., Onodera C.S., Deng J.M., Akiyama K., Ansari Y., RA Arakawa T., Banh J., Banno F., Bowser L., Brooks S.Y., Carninci P., RA Chao Q., Choy N., Enju A., Goldsmith A.D., Gurjal M., Hansen N.F., RA Hayashizaki Y., Johnson-Hopson C., Hsuan V.W., Iida K., Karnes M., RA Khan S., Koesema E., Ishida J., Jiang P.X., Jones T., Kawai J., RA Kamiya A., Meyers C., Nakajima M., Narusaka M., Seki M., Sakurai T., RA Satou M., Tamse R., Vaysberg M., Wallender E.K., Wong C., Yamamura Y., RA Yuan S., Shinozaki K., Davis R.W., Theologis A., Ecker J.R.; RT "Empirical analysis of transcriptional activity in the Arabidopsis RT genome."; RL Science 302:842-846(2003). RN [4] 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 [5] RP X-RAY CRYSTALLOGRAPHY (2.1 ANGSTROMS) OF 7-199. RX MEDLINE=95360746; 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 RT (TBP)."; RL Nat. Struct. Biol. 1:621-637(1994). RN [6] RP X-RAY CRYSTALLOGRAPHY (2.7 ANGSTROMS) OF COMPLEX WITH TFIIB. RX MEDLINE=95405464; 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 [7] RP X-RAY CRYSTALLOGRAPHY (1.9 ANGSTROMS). RX MEDLINE=20084998; 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 CC of the DNA-binding multiprotein factor TFIID. Binding of TFIID to CC the TATA box is the initial transcriptional step of the pre- CC initiation complex (PIC), playing a role in the activation of CC eukaryotic genes transcribed by RNA polymerase II. CC -!- SUBUNIT: Belongs to the TFIID complex together with the TBP- CC associated factors (TAFs). Binds DNA as monomer. CC -!- INTERACTION: CC P41151:HSFA1A; NbExp=1; IntAct=EBI-1544946, EBI-1544927; CC -!- SUBCELLULAR LOCATION: Nucleus. CC -!- ALTERNATIVE PRODUCTS: CC Event=Alternative splicing; Named isoforms=1; CC Comment=A number of isoforms are produced. According to EST CC sequences; CC Name=1; CC IsoId=P28147-1; Sequence=Displayed; CC -!- SIMILARITY: Belongs to the TBP family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; X54996; CAA38743.1; -; mRNA. DR EMBL; AP000603; BAB01751.1; -; 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 PIR; S10946; S10946. DR RefSeq; NP_187953.1; -. DR UniGene; At.24512; -. 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 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 IntAct; P28147; -. DR GeneID; 820546; -. DR GenomeReviews; BA000014_GR; AT3G13445. DR TAIR; At3g13445; -. DR LinkHub; P28147; -. DR ArrayExpress; P28147; -. DR GO; GO:0005669; C:transcription factor TFIID complex; IEA:InterPro. DR GO; GO:0003677; F:DNA binding; IEA:InterPro. DR GO; GO:0005515; F:protein binding; IPI:IntAct. DR GO; GO:0003702; F:RNA polymerase II transcription factor acti...; IEA:InterPro. DR GO; GO:0006355; P:regulation of transcription, DNA-dependent; IEA:InterPro. DR GO; GO:0006367; P:transcription initiation from RNA polymeras...; IEA:InterPro. DR InterPro; IPR012295; b_Adaptin_TBP_C. DR InterPro; IPR000814; TBP. DR Gene3D; G3DSA:3.30.310.10; b_Adaptin_TBP_C; 2. DR PANTHER; PTHR10126; TBP; 1. DR Pfam; PF00352; TBP; 2. DR PRINTS; PR00686; TIFACTORIID. DR PROSITE; PS00351; TFIID; 2. PE 1: Evidence at protein level; KW 3D-structure; Alternative splicing; Complete proteome; DNA-binding; KW Nucleus; Repeat; Transcription. FT CHAIN 1 200 TATA-box-binding protein 1. FT /FTId=PRO_0000153976. FT REPEAT 25 101 1. FT REPEAT 115 192 2. FT STRAND 24 33 FT HELIX 40 46 FT TURN 54 56 FT STRAND 58 64 FT TURN 65 68 FT STRAND 69 73 FT STRAND 77 86 FT HELIX 87 103 FT STRAND 111 123 FT HELIX 130 136 FT TURN 137 140 FT TURN 145 147 FT STRAND 149 155 FT TURN 156 159 FT STRAND 160 164 FT STRAND 168 177 FT HELIX 178 194 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 //