[1]	NUCLEOTIDE SEQUENCE. DOI=10.1038/346390a0; PubMed=2197561 [NCBI, ExPASy, EBI, Israel, Japan] Gasch A., Hoffmann A., Horikoshi M., Roeder R.G., Chua N.-H.; "Arabidopsis thaliana contains two genes for TFIID."; Nature 346:390-394(1990).
[2]	NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. STRAIN=cv. Columbia; DOI=10.1093/dnares/7.3.217; PubMed=10907853 [NCBI, ExPASy, EBI, Israel, Japan] Kaneko T., Katoh T., Sato S., Nakamura Y., Asamizu E., Tabata S.; "Structural analysis of Arabidopsis thaliana chromosome 3. II. Sequence features of the 4,251,695 bp regions covered by 90 P1, TAC and BAC clones."; DNA Res. 7:217-221(2000).
[3]	NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. STRAIN=cv. Columbia; DOI=10.1126/science.1088305; PubMed=14593172 [NCBI, ExPASy, EBI, Israel, Japan] Yamada K., Lim J., Dale J.M., Chen H., Shinn P., Palm C.J., Southwick A.M., Wu H.C., Kim C.J., Nguyen M., Pham P.K., Cheuk R.F., Karlin-Newmann G., Liu S.X., Lam B., Sakano H., Wu T., Yu G., Miranda M., Quach H.L., Tripp M., Chang C.H., Lee J.M., Toriumi M.J., Chan M.M., Tang C.C., Onodera C.S., Deng J.M., Akiyama K., Ansari Y., Arakawa T., Banh J., Banno F., Bowser L., Brooks S.Y., Carninci P., Chao Q., Choy N., Enju A., Goldsmith A.D., Gurjal M., Hansen N.F., Hayashizaki Y., Johnson-Hopson C., Hsuan V.W., Iida K., Karnes M., Khan S., Koesema E., Ishida J., Jiang P.X., Jones T., Kawai J., Kamiya A., Meyers C., Nakajima M., Narusaka M., Seki M., Sakurai T., Satou M., Tamse R., Vaysberg M., Wallender E.K., Wong C., Yamamura Y., Yuan S., Shinozaki K., Davis R.W., Theologis A., Ecker J.R.; "Empirical analysis of transcriptional activity in the Arabidopsis genome."; Science 302:842-846(2003).
[4]	NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. Brover V.V., Troukhan M.E., Alexandrov N.A., Lu Y.-P., Flavell R.B., Feldmann K.A.; "Full-length cDNA from Arabidopsis thaliana."; Submitted (MAR-2002) to the EMBL/GenBank/DDBJ databases.
[5]	X-RAY CRYSTALLOGRAPHY (2.1 ANGSTROMS) OF 7-199. DOI=10.1038/nsb0994-621; PubMed=7634102 [NCBI, ExPASy, EBI, Israel, Japan] Nikolov D.B., Burley S.K.; "2.1 A resolution refined structure of a TATA box-binding protein (TBP)."; Nat. Struct. Biol. 1:621-637(1994).
[6]	X-RAY CRYSTALLOGRAPHY (2.7 ANGSTROMS) OF COMPLEX WITH TFIIB. DOI=10.1038/377119a0; PubMed=7675079 [NCBI, ExPASy, EBI, Israel, Japan] Nikolov D.B., Chen H., Halay E.D., Usheva A.A., Hisatake K., Lee D.K., Roeder R.G., Burley S.K.; "Crystal structure of a TFIIB-TBP-TATA-element ternary complex."; Nature 377:119-128(1995).
[7]	X-RAY CRYSTALLOGRAPHY (1.9 ANGSTROMS). DOI=10.1101/gad.13.24.3217; PubMed=10617571 [NCBI, ExPASy, EBI, Israel, Japan] Patikoglou G.A., Kim J.L., Sun L., Yang S.H., Kodadek T., Burley S.K.; "TATA element recognition by the TATA box-binding protein has been conserved throughout evolution."; Genes Dev. 13:3217-3230(1999).

Comments

FUNCTION: General transcription factor that functions at the core of the DNA-binding multiprotein factor TFIID. Binding of TFIID to the TATA box is the initial transcriptional step of the pre-initiation complex (PIC), playing a role in the activation of eukaryotic genes transcribed by RNA polymerase II.
SUBUNIT: Belongs to the TFIID complex together with the TBP-associated factors (TAFs). Binds DNA as monomer.
INTERACTION:
P41151:HSFA1A; NbExp=1; IntAct=EBI-1544946, EBI-1544927;
SUBCELLULAR LOCATION: Nucleus.
ALTERNATIVE PRODUCTS: 1 named isoform [FASTA] produced by alternative splicing. A number of isoforms are produced. According to EST sequences.

Name 1

Isoform ID P28147-1

This is the isoform sequence displayed in this entry.
SIMILARITY: Belongs to the TBP family.

Copyright

Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms. Distributed under the Creative Commons Attribution-NoDerivs License.

Cross-references

Sequence databases

EMBL

X54996; CAA38743.1; -; mRNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
AP000603; BAB01751.1; -; Genomic_DNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
AF324696; AAG40047.1; -; mRNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
AF327429; AAG42019.1; -; mRNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
AF349523; AAK15570.1; -; mRNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
AY054608; AAK96799.1; -; mRNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
AY072455; AAL66870.1; -; mRNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
AY084881; AAM61444.1; -; mRNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]

S10946; S10946.

NP_187953.1; -.

3D structure databases

PDB

1QN3; X-ray; 1.95 A; A/B=1-200.	[ExPASy / RCSB / EBI]
1QN4; X-ray; 1.86 A; A/B=1-200.	[ExPASy / RCSB / EBI]
1QN5; X-ray; 1.93 A; A/B=1-200.	[ExPASy / RCSB / EBI]
1QN6; X-ray; 2.10 A; A/B=1-200.	[ExPASy / RCSB / EBI]
1QN7; X-ray; 2.30 A; A/B=1-200.	[ExPASy / RCSB / EBI]
1QN8; X-ray; 2.10 A; A/B=1-200.	[ExPASy / RCSB / EBI]
1QN9; X-ray; 1.90 A; A/B=1-200.	[ExPASy / RCSB / EBI]
1QNA; X-ray; 1.80 A; A/B=1-200.	[ExPASy / RCSB / EBI]
1QNB; X-ray; 2.23 A; A/B=1-200.	[ExPASy / RCSB / EBI]
1QNC; X-ray; 2.30 A; A/B=1-200.	[ExPASy / RCSB / EBI]
1QNE; X-ray; 1.90 A; A/B=1-200.	[ExPASy / RCSB / EBI]
1VOK; X-ray; 2.10 A; A/B=1-200.	[ExPASy / RCSB / EBI]
1VOL; X-ray; 2.70 A; B=1-200.	[ExPASy / RCSB / EBI]

Detailed list of linked structures.

PDBsum

1QN3; -.
1QN4; -.
1QN5; -.
1QN6; -.
1QN7; -.
1QN8; -.
1QN9; -.
1QNA; -.
1QNB; -.
1QNC; -.
1QNE; -.
1VOK; -.
1VOL; -.

ModBase

P28147.

Protein-protein interaction databases

IntAct

P28147; -.

Organism-specific databases

TAIR

At3g13445; -.

Gene expression databases

ArrayExpress

P28147; -.

Ontologies

GO:0005515;	Molecular function: protein binding (inferred from physical interaction from IntAct).
QuickGo view.

Family and domain databases

InterPro

IPR012295; b_Adaptin_TBP_C.
IPR000814; TBP.
Graphical view of domain structure.

Gene3D

G3DSA:3.30.310.10; b_Adaptin_TBP_C; 2.

PANTHER

PTHR10126; TBP; 1.

Pfam

PF00352; TBP; 2.
Pfam graphical view of domain structure.

PRINTS

PR00686; TIFACTORIID.

PROSITE

PS00351; TFIID; 2.

BLOCKS

P28147.

Genome annotation databases

GeneID

820546; -.

GenomeReviews

BA000014_GR; AT3G13445.

Other

P28147; -.

View cluster of proteins with at least 50% / 90% / 100% identity.

Keywords

3D-structure; Alternative splicing; Complete proteome; DNA-binding; Nucleus; Repeat; Transcription.

Features

Feature table viewer

Feature aligner

`Key`	`From To`	`Length`	`Description`	`FTId`
`CHAIN`	`1 200`	`200`	`TATA-box-binding protein 1.`	`PRO_0000153976`
`REPEAT`	`25 101`	`77`	`1.`
`REPEAT`	`115 192`	`78`	`2.`
`STRAND`	`24 33`	`10`
`HELIX`	`40 46`	`7`
`TURN`	`54 56`	`3`
`STRAND`	`58 64`	`7`
`TURN`	`65 68`	`4`
`STRAND`	`69 73`	`5`
`STRAND`	`77 86`	`10`
`HELIX`	`87 103`	`17`
`STRAND`	`111 123`	`13`
`HELIX`	`130 136`	`7`
`TURN`	`137 140`	`4`
`TURN`	`145 147`	`3`
`STRAND`	`149 155`	`7`
`TURN`	`156 159`	`4`
`STRAND`	`160 164`	`5`
`STRAND`	`168 177`	`10`
`HELIX`	`178 194`	`17`

Sequence information

Length: 200 AA [This is the length of the unprocessed precursor]

Molecular weight: 22368 Da [This is the MW of the unprocessed precursor]

CRC64: 9E15DC2308818919 [This is a checksum on the sequence]

        10         20         30         40         50         60 
MTDQGLEGSN PVDLSKHPSG IVPTLQNIVS TVNLDCKLDL KAIALQARNA EYNPKRFAAV 

        70         80         90        100        110        120 
IMRIREPKTT ALIFASGKMV CTGAKSEDFS KMAARKYARI VQKLGFPAKF KDFKIQNIVG 

       130        140        150        160        170        180 
SCDVKFPIRL EGLAYSHAAF SSYEPELFPG LIYRMKVPKI VLLIFVSGKI VITGAKMRDE 

       190        200 
TYKAFENIYP VLSEFRKIQQ

P28147 in FASTA format

View entry in original UniProtKB/Swiss-Prot format
View entry in raw text format (no links)
Report form for errors/updates in this UniProtKB/Swiss-Prot entry

	BLAST submission on ExPASy/SIB or at NCBI (USA)		Sequence analysis tools: ProtParam, ProtScale, Compute pI/Mw, PeptideMass, PeptideCutter, Dotlet (Java)
	ScanProsite, MotifScan		Submit a homology modeling request to SWISS-MODEL
	NPSA Sequence analysis tools