P20226 (TBP_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
TATA-box-binding protein

Alternative name(s):
TATA sequence-binding protein
TATA-binding factor
TATA-box factor
Transcription initiation factor TFIID TBP subunit

Gene names

Name:	TBP
Synonyms:	GTF2D1, TF2D, TFIID

Organism

Homo sapiens (Human)

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Primates › Haplorrhini › Catarrhini › Hominidae › Homo

Protein attributes

Sequence length	339 AA.
Sequence status	Complete.
Protein existence	Evidence at protein level

General annotation (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. Component of the transcription factor SL1/TIF-IB complex, which is involved in the assembly of the PIC (preinitiation complex) during RNA polymerase I-dependent transcription. The rate of PIC formation probably is primarily dependent on the rate of association of SL1 with the rDNA promoter. SL1 is involved in stabilization of nucleolar transcription factor 1/UBTF on rDNA. Ref.12
Subunit structure	Binds DNA as monomer. Belongs to the TFIID complex together with the TBP-associated factors (TAFs). Component of the transcription factor SL1/TIF-IB complex, composed of TBP and at least TAF1A, TAF1B TAF1C and TAF1D. Association of TBP to form either TFIID or SL1/TIF-IB appears to be mutually exclusive. Interacts with TAF1A, TAF1B and TAF1C. Interacts with TFIIB, NCOA6, DRAP1, DR1 and ELF3. Interacts with SPIB, SNAPC1, SNAPC2 and SNAPC4. Interacts with UTF1. Interacts with BRF2. Interacts with UBTF. Interacts with GPBP1. Interacts with CITED2 By similarity. Interacts with ATF7IP. Interacts with HIV-1 Tat. Ref.6 Ref.7 Ref.8 Ref.9 Ref.10 Ref.14 Ref.15 Ref.16 Ref.17 Ref.18 Ref.19 Ref.20 Ref.21 Ref.22
Subcellular location	Nucleus.
Tissue specificity	Widely expressed, with levels highest in the testis and ovary. Ref.13
Polymorphism	The poly-Gln region of TBP is highly polymorphic (25 to 42 repeats) in normal individuals and is expanded to about 47-63 repeats in spinocerebellar ataxia 17 (SCA17) patients.
Involvement in disease	Defects in TBP are the cause of spinocerebellar ataxia type 17 (SCA17) [MIM:607136]. Spinocerebellar ataxia is a clinically and genetically heterogeneous group of cerebellar disorders. Patients show progressive incoordination of gait and often poor coordination of hands, speech and eye movements, due to degeneration of the cerebellum with variable involvement of the brainstem and spinal cord. SCA17 is an autosomal dominant cerebellar ataxia (ADCA) characterized by widespread cerebral and cerebellar atrophy, dementia and extrapyramidal signs. The molecular defect in SCA17 is the expansion of a CAG repeat in the coding region of TBP. Longer expansions result in earlier onset and more severe clinical manifestations of the disease. Ref.29 Ref.30 Ref.31
Sequence similarities	Belongs to the TBP family.

Ontologies

Keywords
Biological process	Host-virus interaction Transcription Transcription regulation
Cellular component	Nucleus
Coding sequence diversity	Polymorphism Triplet repeat expansion
Disease	Disease mutation Neurodegeneration Spinocerebellar ataxia
Domain	Repeat
Ligand	DNA-binding
Technical term	3D-structure Complete proteome Reference proteome
Gene Ontology (GO)
Biological process	cell death Inferred from electronic annotation. Source: UniProtKB-KW interspecies interaction between organisms Inferred from electronic annotation. Source: UniProtKB-KW transcription elongation from RNA polymerase II promoter Traceable author statement. Source: Reactome transcription from RNA polymerase III promoter Inferred from direct assay. Source: MGI transcription initiation from RNA polymerase II promoter Inferred by curator. Source: UniProtKB viral reproduction Traceable author statement. Source: Reactome
Cellular component	transcription factor TFIIA complex Inferred from direct assay. Source: BHF-UCL transcription factor TFIID complex Inferred from direct assay. Source: UniProtKB
Molecular function	repressing transcription factor binding Inferred from physical interaction. Source: BHF-UCL transcription regulatory region DNA binding Inferred from direct assay. Source: UniProtKB
Complete GO annotation...

Binary interactions

With	Entry	#Exp.	IntAct	Notes
EDF1	O60869-1	2	EBI-355371,EBI-781310
GTF2A2	P52657	2	EBI-355371,EBI-1045262
POU3F2	P20265	2	EBI-355371,EBI-1167176
TAF1	P21675	5	EBI-355371,EBI-491289
TP53	P04637	2	EBI-355371,EBI-366083

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 339

339

TATA-box-binding protein

PRO_0000153956

Regions

Repeat

165 – 241

77

1

Repeat

255 – 332

78

2

Compositional bias

55 – 95

41

Poly-Gln

Natural variations

Natural variant

92 – 95

4

Missing.

VAR_016987

Experimental info

Sequence conflict

187

1

A → R in AAC03409. Ref.3

Secondary structure

1

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339

Helix Strand Turn

Details...

Beta strand

164 – 173

10

Helix

180 – 186

7

Beta strand

190 – 192

3

Turn

194 – 196

3

Beta strand

198 – 204

7

Turn

205 – 208

4

Beta strand

209 – 213

5

Beta strand

217 – 222

6

Helix

227 – 244

18

Beta strand

251 – 263

13

Helix

270 – 276

7

Turn

277 – 280

4

Turn

285 – 287

3

Beta strand

289 – 295

7

Turn

296 – 299

4

Beta strand

300 – 304

5

Beta strand

308 – 313

6

Helix

318 – 333

16

Sequences

	Sequence		Length	Mass (Da)
	P20226 [UniParc]. Last modified February 1, 1996. Version 2. Checksum: A61A578D972B970B	FASTA	339	37,698
	10 20 30 40 50 60 MDQNNSLPPY AQGLASPQGA MTPGIPIFSP MMPYGTGLTP QPIQNTNSLS ILEEQQRQQQ 70 80 90 100 110 120 QQQQQQQQQQ QQQQQQQQQQ QQQQQQQQQQ QQQQQAVAAA AVQQSTSQQA TQGTSGQAPQ 130 140 150 160 170 180 LFHSQTLTTA PLPGTTPLYP SPMTPMTPIT PATPASESSG IVPQLQNIVS TVNLGCKLDL 190 200 210 220 230 240 KTIALRARNA EYNPKRFAAV IMRIREPRTT ALIFSSGKMV CTGAKSEEQS RLAARKYARV 250 260 270 280 290 300 VQKLGFPAKF LDFKIQNMVG SCDVKFPIRL EGLVLTHQQF SSYEPELFPG LIYRMIKPRI 310 320 330 VLLIFVSGKV VLTGAKVRAE IYEAFENIYP ILKGFRKTT

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Highly conserved core domain and unique N-terminus with presumptive regulatory motifs in a human TATA factor (TFIID)." Hoffmann A., Sinn E., Yamamoto T., Wang J., Roy A., Horikoshi M., Roeder R.G. Nature 346:387-390(1990) [PubMed: 2374612] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA], VARIANT 92-GLN--GLN-95 DEL.
[2]	"Functional domains and upstream activation properties of cloned human TATA binding protein." Peterson M.G., Tanese N., Pugh B.F., Tjian R. Science 248:1625-1630(1990) [PubMed: 2363050] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA], DOMAINS.
[3]	"Cloning of a transcriptionally active human TATA binding factor." Kao C.C., Lieberman P.M., Schmidt M.C., Zhou Q., Pei R., Berk A.J. Science 248:1646-1650(1990) [PubMed: 2194289] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA]. Tissue: Fibroblast.
[4]	"Cloning of human full open reading frames in Gateway(TM) system entry vector (pDONR201)." Ebert L., Schick M., Neubert P., Schatten R., Henze S., Korn B. Submitted (JUN-2004) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
[5]	"The DNA sequence and analysis of human chromosome 6." Mungall A.J., Palmer S.A., Sims S.K., Edwards C.A., Ashurst J.L., Wilming L., Jones M.C., Horton R., Hunt S.E., Scott C.E., Gilbert J.G.R., Clamp M.E., Bethel G., Milne S., Ainscough R., Almeida J.P., Ambrose K.D., Andrews T.D. , Ashwell R.I.S., Babbage A.K., Bagguley C.L., Bailey J., Banerjee R., Barker D.J., Barlow K.F., Bates K., Beare D.M., Beasley H., Beasley O., Bird C.P., Blakey S.E., Bray-Allen S., Brook J., Brown A.J., Brown J.Y., Burford D.C., Burrill W., Burton J., Carder C., Carter N.P., Chapman J.C., Clark S.Y., Clark G., Clee C.M., Clegg S., Cobley V., Collier R.E., Collins J.E., Colman L.K., Corby N.R., Coville G.J., Culley K.M., Dhami P., Davies J., Dunn M., Earthrowl M.E., Ellington A.E., Evans K.A., Faulkner L., Francis M.D., Frankish A., Frankland J., French L., Garner P., Garnett J., Ghori M.J., Gilby L.M., Gillson C.J., Glithero R.J., Grafham D.V., Grant M., Gribble S., Griffiths C., Griffiths M.N.D., Hall R., Halls K.S., Hammond S., Harley J.L., Hart E.A., Heath P.D., Heathcott R., Holmes S.J., Howden P.J., Howe K.L., Howell G.R., Huckle E., Humphray S.J., Humphries M.D., Hunt A.R., Johnson C.M., Joy A.A., Kay M., Keenan S.J., Kimberley A.M., King A., Laird G.K., Langford C., Lawlor S., Leongamornlert D.A., Leversha M., Lloyd C.R., Lloyd D.M., Loveland J.E., Lovell J., Martin S., Mashreghi-Mohammadi M., Maslen G.L., Matthews L., McCann O.T., McLaren S.J., McLay K., McMurray A., Moore M.J.F., Mullikin J.C., Niblett D., Nickerson T., Novik K.L., Oliver K., Overton-Larty E.K., Parker A., Patel R., Pearce A.V., Peck A.I., Phillimore B.J.C.T., Phillips S., Plumb R.W., Porter K.M., Ramsey Y., Ranby S.A., Rice C.M., Ross M.T., Searle S.M., Sehra H.K., Sheridan E., Skuce C.D., Smith S., Smith M., Spraggon L., Squares S.L., Steward C.A., Sycamore N., Tamlyn-Hall G., Tester J., Theaker A.J., Thomas D.W., Thorpe A., Tracey A., Tromans A., Tubby B., Wall M., Wallis J.M., West A.P., White S.S., Whitehead S.L., Whittaker H., Wild A., Willey D.J., Wilmer T.E., Wood J.M., Wray P.W., Wyatt J.C., Young L., Younger R.M., Bentley D.R., Coulson A., Durbin R.M., Hubbard T., Sulston J.E., Dunham I., Rogers J., Beck S. Nature 425:805-811(2003) [PubMed: 14574404] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[6]	"The RNA polymerase I transcription factor, upstream binding factor, interacts directly with the TATA box-binding protein." Kwon H., Green M.R. J. Biol. Chem. 269:30140-30146(1994) [PubMed: 7982918] [Abstract] Cited for: INTERACTION WITH UBFT.
[7]	"Direct interaction of human TFIID with the HIV-1 transactivator tat." Kashanchi F., Piras G., Radonovich M.F., Duvall J.F., Fattaey A., Chiang C.M., Roeder R.G., Brady J.N. Nature 367:295-299(1994) [PubMed: 8121496] [Abstract] Cited for: INTERACTION WITH HIV-1 TAT.
[8]	"Reconstitution of transcription factor SL1: exclusive binding of TBP by SL1 or TFIID subunits." Comai L., Zomerdijk J.C.B.M., Beckmann H., Zhou S., Admon A., Tjian R. Science 266:1966-1972(1994) [PubMed: 7801123] [Abstract] Cited for: INTERACTION WITH TAF1A; TAF1B AND TAF1C.
[9]	"Evidence for functional interaction between the HIV-1 Tat transactivator and the TATA box binding protein in vivo." Veschambre P., Simard P., Jalinot P. J. Mol. Biol. 250:169-180(1995) [PubMed: 7608968] [Abstract] Cited for: INTERACTION WITH HIV-1 TAT.
[10]	"Characterization of functional domains of an embryonic stem cell coactivator UTF1 which are conserved and essential for potentiation of ATF-2 activity." Fukushima A., Okuda A., Nishimoto M., Seki N., Hori T.A., Muramatsu M. J. Biol. Chem. 273:25840-25849(1998) [PubMed: 9748258] [Abstract] Cited for: INTERACTION WITH UTF1.
[11]	"Requirement of RSF and FACT for transcription of chromatin templates in vitro." LeRoy G., Orphanides G., Lane W.S., Reinberg D. Science 282:1900-1904(1998) [PubMed: 9836642] [Abstract] Cited for: IDENTIFICATION IN THE TFIID COMPLEX.
[12]	"TBP-TAF complex SL1 directs RNA polymerase I pre-initiation complex formation and stabilizes upstream binding factor at the rDNA promoter." Friedrich J.K., Panov K.I., Cabart P., Russell J., Zomerdijk J.C.B.M. J. Biol. Chem. 280:29551-29558(2005) [PubMed: 15970593] [Abstract] Cited for: FUNCTION OF THE SL1/TIF-IB COMPLEX.
[13]	"Genomics, evolution, and expression of TBPL2, a member of the TBP family." Di Pietro C., Ragusa M., Duro L., Guglielmino M.R., Barbagallo D., Carnemolla A., Lagana A., Buffa P., Angelica R., Rinaldi A., Calafato M.S., Milicia I., Caserta C., Giugno R., Pulvirenti A., Giunta V., Rapisarda A., Di Pietro V. , Grillo A., Messina A., Ferro A., Grzeschik K.H., Purrello M. DNA Cell Biol. 26:369-385(2007) [PubMed: 17570761] [Abstract] Cited for: TISSUE SPECIFICITY.
[14]	"SPI-B activates transcription via a unique proline, serine, and threonine domain and exhibits DNA binding affinity differences from PU.1." Rao S., Matsumura A., Yoon J., Simon M.C. J. Biol. Chem. 274:11115-11124(1999) [PubMed: 10196196] [Abstract] Cited for: INTERACTION WITH SPIB.
[15]	"A nuclear factor ASC-2, as a cancer-amplified transcriptional coactivator essential for ligand-dependent transactivation by nuclear receptors in vivo." Lee S.-K., Anzick S.L., Choi J.-E., Bubendorf L., Guan X.-Y., Jung Y.-K., Kallioniemi O.-P., Kononen J., Trent J.M., Azorsa D., Jhun B.-H., Cheong J.H., Lee Y.C., Meltzer P.S., Lee J.W. J. Biol. Chem. 274:34283-34293(1999) [PubMed: 10567404] [Abstract] Cited for: INTERACTION WITH NCOA6.
[16]	"Exon 4-encoded acidic domain in the epithelium-restricted Ets factor, ESX, confers potent transactivating capacity and binds to TATA-binding protein (TBP)." Chang C.-H., Scott G.K., Baldwin M.A., Benz C.C. Oncogene 18:3682-3695(1999) [PubMed: 10391676] [Abstract] Cited for: INTERACTION WITH ELF3.
[17]	"BRFU, a TFIIB-like factor, is directly recruited to the TATA-box of polymerase III small nuclear RNA gene promoters through its interaction with TATA-binding protein." Cabart P., Murphy S. J. Biol. Chem. 276:43056-43064(2001) [PubMed: 11564744] [Abstract] Cited for: INTERACTION WITH BRF2.
[18]	"The TFIID components human TAFII140 and Drosophila BIP2 (TAFII155) are novel metazoan homologues of yeast TAFII47 containing a histone fold and a PHD finger." Gangloff Y.G., Pointud J.-C., Thuault S., Carre L., Romier C., Muratoglu S., Brand M., Tora L., Couderc J.-L., Davidson I. Mol. Cell. Biol. 21:5109-5121(2001) [PubMed: 11438666] [Abstract] Cited for: INTERACTION WITH TAF3.
[19]	"Functional substitution for TAF(II)250 by a retroposed homolog that is expressed in human spermatogenesis." Wang P.J., Page D.C. Hum. Mol. Genet. 11:2341-2346(2002) [PubMed: 12217962] [Abstract] Cited for: INTERACTION WITH TAF1L.
[20]	"The small nuclear RNA-activating protein 190 Myb DNA binding domain stimulates TATA box-binding protein-TATA box recognition." Hinkley C.S., Hirsch H.A., Gu L., LaMere B., Henry R.W. J. Biol. Chem. 278:18649-18657(2003) [PubMed: 12621023] [Abstract] Cited for: INTERACTION WITH SNAPC1; SNAPC2 AND SNAPC4.
[21]	"HIV-1 Tat stimulates transcription complex assembly through recruitment of TBP in the absence of TAFs." Raha T., Cheng S.W.G., Green M.R. PLoS Biol. 3:221-230(2005) [PubMed: 15719058] [Abstract] Cited for: INTERACTION WITH HIV-1 TAT.
[22]	"MCAF1/AM is involved in Sp1-mediated maintenance of cancer-associated telomerase activity." Liu L., Ishihara K., Ichimura T., Fujita N., Hino S., Tomita S., Watanabe S., Saitoh N., Ito T., Nakao M. J. Biol. Chem. 284:5165-5174(2009) [PubMed: 19106100] [Abstract] Cited for: INTERACTION WITH SP1.
[23]	"Initial characterization of the human central proteome." Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J. BMC Syst. Biol. 5:17-17(2011) [PubMed: 21269460] [Abstract] Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[24]	"Crystal structure of a human TATA box-binding protein/TATA element complex." Nikolov D.B., Chen H., Halay E.D., Hoffmann A., Roeder R.G., Burley S.K. Proc. Natl. Acad. Sci. U.S.A. 93:4862-4867(1996) [PubMed: 8643494] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (1.9 ANGSTROMS) OF 159-337 IN COMPLEX WITH DNA.
[25]	"How proteins recognize the TATA box." Juo Z.S., Chiu T.K., Leiberman P.M., Baikalov I., Berk A.J., Dickerson R.E. J. Mol. Biol. 261:239-254(1996) [PubMed: 8757291] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (2.9 ANGSTROMS) OF 159-339 IN COMPLEX WITH DNA.
[26]	"Structural basis of preinitiation complex assembly on human pol II promoters." Tsai F.T.F., Sigler P.B. EMBO J. 19:25-36(2000) [PubMed: 10619841] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (2.65 ANGSTROMS) OF 159-337 IN COMPLEX WITH GTF2B AND DNA.
[27]	"Crystal structure of negative cofactor 2 recognizing the TBP-DNA transcription complex." Kamada K., Shu F., Chen H., Malik S., Stelzer G., Roeder R.G., Meisterernst M., Burley S.K. Cell 106:71-81(2001) [PubMed: 11461703] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (2.62 ANGSTROMS) OF 159-339 IN COMPLEX WITH DR1; DRAP1 AND DNA.
[28]	"A neurological disease caused by an expanded CAG trinucleotide repeat in the TATA-binding protein gene: a new polyglutamine disease?" Koide R., Kobayashi S., Shimohata T., Ikeuchi T., Maruyama M., Saito M., Yamada M., Takahashi H., Tsuji S. Hum. Mol. Genet. 8:2047-2053(1999) [PubMed: 10484774] [Abstract] Cited for: POLYMORPHISM OF POLY-GLN REGION.
[29]	"Different types of repeat expansion in the TATA-binding protein gene are associated with a new form of inherited ataxia." Zuhlke C., Hellenbroich Y., Dalski A., Kononowa N., Hagenah J., Vieregge P., Riess O., Klein C., Schwinger E. Eur. J. Hum. Genet. 9:160-164(2001) [PubMed: 11313753] [Abstract] Cited for: POLYMORPHISM OF POLY-GLN REGION, INVOLVEMENT IN SCA17.
[30]	"SCA17, a novel autosomal dominant cerebellar ataxia caused by an expanded polyglutamine in TATA-binding protein." Nakamura K., Jeong S.-Y., Uchihara T., Anno M., Nagashima K., Nagashima T., Ikeda S., Tsuji S., Kanazawa I. Hum. Mol. Genet. 10:1441-1448(2001) [PubMed: 11448935] [Abstract] Cited for: POLYMORPHISM OF POLY-GLN REGION, INVOLVEMENT IN SCA17.
[31]	"Trinucleotide repeats in 202 families with ataxia: a small expanded (CAG)n allele at the SCA17 locus." Silveira I., Miranda C., Guimaraes L., Moreira M.-C., Alonso I., Mendonca P., Ferro A., Pinto-Basto J., Coelho J., Ferreirinha F., Poirier J., Parreira E., Vale J., Januario C., Barbot C., Tuna A., Barros J., Koide R. , Tsuji S., Holmes S.E., Margolis R.L., Jardim L., Pandolfo M., Coutinho P., Sequeiros J. Arch. Neurol. 59:623-629(2002) [PubMed: 11939898] [Abstract] Cited for: POLYMORPHISM OF POLY-GLN REGION, INVOLVEMENT IN SCA17.
+	Additional computationally mapped references.

Web resources

GeneReviews

Cross-references

Sequence databases

EMBL
GenBank
DDBJ

X54993 mRNA. Translation: CAA38736.1.
M55654 mRNA. Translation: AAA36731.1.
M34960 mRNA. Translation: AAC03409.1.
CR456776 mRNA. Translation: CAG33057.1.
AL031259 Genomic DNA. Translation: CAA20286.1.

IPI

IPI00022831.

PIR

TWHU2D. A34830.

RefSeq

NP_003185.1. NM_003194.4.

UniGene

Hs.590872.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
1C9B	X-ray	2.65	B/F/J/N/R	159-337	[»]
1CDW	X-ray	1.90	A	159-337	[»]
1JFI	X-ray	2.62	C	159-339	[»]
1NVP	X-ray	2.10	A	159-339	[»]
1TGH	X-ray	2.90	A	159-339	[»]

ProteinModelPortal

P20226.

SMR

P20226. Positions 159-337.

ModBase

Search...

Protein-protein interaction databases

DIP

DIP-1078N.

IntAct

P20226. 34 interactions.

MINT

MINT-156456.

STRING

P20226.

PTM databases

PhosphoSite

P20226.

Polymorphism databases

DMDM

1351223.

Proteomic databases

PRIDE

P20226.

Protocols and materials databases

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

Ensembl

ENST00000230354; ENSP00000230354; ENSG00000112592.
ENST00000392092; ENSP00000375942; ENSG00000112592.

GeneID

6908.

KEGG

hsa:6908.

UCSC

uc003qxt.1. human.

Organism-specific databases

CTD

6908.

GeneCards

GC06P170781.

H-InvDB

HIX0032941.

HGNC

HGNC:11588. TBP.

HPA

CAB009442.

MIM

600075. gene.
607136. phenotype.

neXtProt

NX_P20226.

Orphanet

98759. Spinocerebellar ataxia type 17.

GenAtlas

Search...

Phylogenomic databases

eggNOG

prNOG12350.

HOGENOM

HBG499930.

HOVERGEN

HBG044997.

InParanoid

P20226.

OMA

PMMPYGT.

PhylomeDB

P20226.

Enzyme and pathway databases

Reactome

REACT_1788. Transcription.
REACT_6185. HIV Infection.
REACT_71. Gene Expression.

Gene expression databases

ArrayExpress

P20226.

Bgee

P20226.

CleanEx

HS_TBP.

Genevestigator

P20226.

GermOnline

ENSG00000112592. Homo sapiens.

Family and domain databases

InterPro

IPR011989. ARM-like.
IPR000814. TBP.
IPR012294. TFIID_C/glycos_N.
[Graphical view]

Gene3D

G3DSA:1.25.10.10. ARM-like. 1 hit.

KO

K03120.

PANTHER

PTHR10126. TBP. 1 hit.

Pfam

PF00352. TBP. 2 hits.
[Graphical view]

PRINTS

PR00686. TIFACTORIID.

SUPFAM

SSF55945. TFIID_C/glycos_N. 2 hits.

PROSITE

PS00351. TFIID. 2 hits.
[Graphical view]

ProtoNet

Search...

Other

NextBio

27015.

SOURCE

Search...

Entry information

Entry name

TBP_HUMAN

Accession

Primary (citable) accession number: P20226
Secondary accession number(s): Q16845, Q6IBM6, Q9UC02

Entry history

Integrated into UniProtKB/Swiss-Prot:	February 1, 1991
Last sequence update:	February 1, 1996
Last modified:	January 25, 2012
This is version 147 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program

Disclaimer

Any medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.