Q00403 (TF2B_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Transcription initiation factor IIB

Alternative name(s):
General transcription factor TFIIB
S300-II

Gene names

Name:	GTF2B
Synonyms:	TF2B, TFIIB

Organism

Homo sapiens (Human) [Reference proteome]

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Deuterostomia › Chordata › Craniata › Vertebrata › Gnathostomata › Teleostomi › Euteleostomi › Sarcopterygii › Tetrapoda › Amniota › Mammalia › Theria › Eutheria › Euarchontoglires › Primates › Haplorrhini › Simiiformes › Catarrhini › Hominoidea › Hominidae › Homininae › Homo

Protein attributes

Sequence length	316 AA.
Sequence status	Complete.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	General factor that plays a major role in the activation of eukaryotic genes transcribed by RNA polymerase II.
Cofactor	Binds 1 zinc ion per subunit.
Subunit structure	Associates with TFIID-IIA (DA complex) to form TFIID-IIA-IIB (DAB-complex) which is then recognized by polymerase II. Interacts with the transcription elongation factor TCEA2. Interacts with HIV-1 Vpr. Interacts with GPBP1 By similarity. Interacts with Epstein-Barr virus EBNA2. Ref.8 Ref.9 Ref.10
Subcellular location	Nucleus.
Sequence similarities	Belongs to the TFIIB family. Contains 1 TFIIB-type zinc finger.

Ontologies

Keywords
Biological process	Host-virus interaction Transcription Transcription regulation
Cellular component	Nucleus
Coding sequence diversity	Polymorphism
Domain	Repeat Zinc-finger
Ligand	Metal-binding Zinc
PTM	Phosphoprotein
Technical term	3D-structure Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	regulation of transcription, DNA-dependent Inferred from electronic annotation. Source: UniProtKB-KW transcription elongation from RNA polymerase II promoter Traceable author statement. Source: Reactome transcription initiation from RNA polymerase II promoter Traceable author statement. Source: Reactome viral reproduction Traceable author statement. Source: Reactome virus-host interaction Inferred from electronic annotation. Source: UniProtKB-KW
Cellular_component	nucleoplasm Traceable author statement. Source: Reactome
Molecular_function	DNA binding Inferred from electronic annotation. Source: Compara zinc ion binding Inferred from electronic annotation. Source: InterPro
Complete GO annotation...

Binary interactions

With	Entry	#Exp.	IntAct	Notes
GRF4	P46077	2	EBI-389564,EBI-637479	From a different organism.
Vdr	P48281	2	EBI-389564,EBI-346797	From a different organism.

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 316

316

Transcription initiation factor IIB

PRO_0000119293

Regions

Repeat

124 – 200

77

1

Repeat

218 – 294

77

2

Zinc finger

11 – 42

32

TFIIB-type

Sites

Metal binding

15

1

Zinc

Metal binding

18

1

Zinc

Metal binding

34

1

Zinc

Metal binding

37

1

Zinc

Amino acid modifications

Modified residue

76

1

Phosphoserine Ref.12 Ref.13

Natural variations

Natural variant

19

1

P → S.
Corresponds to variant rs1804499 [ dbSNP | Ensembl ].

VAR_011977

Natural variant

132

1

R → Q in a colorectal cancer sample; somatic mutation. Ref.18

VAR_035722

Experimental info

Mutagenesis

51 – 56

6

EWRTFS → AWRTFA: Partial loss of HIV-1 Vpr binding.

Mutagenesis

52

1

W → A: Partial loss of HIV-1 Vpr binding.

Mutagenesis

53 – 54

2

RT → AA: Partial loss of HIV-1 Vpr binding.

Mutagenesis

55

1

F → A: Partial loss of HIV-1 Vpr binding.

Secondary structure

1

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316

Helix Strand Turn

Details...

Beta strand

4 – 6

3

Beta strand

18 – 21

4

Beta strand

24 – 26

3

Beta strand

27 – 29

3

Turn

35 – 37

3

Helix

111 – 113

3

Helix

114 – 127

14

Helix

132 – 148

17

Beta strand

152 – 154

3

Helix

156 – 170

15

Helix

177 – 182

6

Beta strand

184 – 186

3

Helix

188 – 201

14

Helix

212 – 221

10

Helix

226 – 241

16

Helix

250 – 263

14

Beta strand

265 – 267

3

Helix

271 – 278

8

Helix

282 – 292

11

Helix

293 – 295

3

Helix

296 – 299

4

Helix

310 – 312

3

Sequences

	Sequence		Length	Mass (Da)
	Q00403 [UniParc]. Last modified December 1, 1992. Version 1. Checksum: 9CC7E102526C2722	FASTA	316	34,833
	10 20 30 40 50 60 MASTSRLDAL PRVTCPNHPD AILVEDYRAG DMICPECGLV VGDRVIDVGS EWRTFSNDKA 70 80 90 100 110 120 TKDPSRVGDS QNPLLSDGDL STMIGKGTGA ASFDEFGNSK YQNRRTMSSS DRAMMNAFKE 130 140 150 160 170 180 ITTMADRINL PRNIVDRTNN LFKQVYEQKS LKGRANDAIA SACLYIACRQ EGVPRTFKEI 190 200 210 220 230 240 CAVSRISKKE IGRCFKLILK ALETSVDLIT TGDFMSRFCS NLCLPKQVQM AATHIARKAV 250 260 270 280 290 300 ELDLVPGRSP ISVAAAAIYM ASQASAEKRT QKEIGDIAGV ADVTIRQSYR LIYPRAPDLF 310 PTDFKFDTPV DKLPQL

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Cloning of a human gene encoding the general transcription initiation factor IIB." Ha I., Lane W.S., Reinberg D. Nature 352:689-695(1991) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA].
[2]	"Sequence of general transcription factor TFIIB and relationships to other initiation factors." Malik S., Hisatake K., Sumimoto H., Horikoshi M., Roeder R.G. Proc. Natl. Acad. Sci. U.S.A. 88:9553-9557(1991) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA].
[3]	"Complete sequencing and characterization of 21,243 full-length human cDNAs." Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S. , Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S. Nat. Genet. 36:40-45(2004) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. Tissue: Brain.
[4]	"Human protein factory for converting the transcriptome into an in vitro-expressed proteome." Goshima N., Kawamura Y., Fukumoto A., Miura A., Honma R., Satoh R., Wakamatsu A., Yamamoto J., Kimura K., Nishikawa T., Andoh T., Iida Y., Ishikawa K., Ito E., Kagawa N., Kaminaga C., Kanehori K., Kawakami B. , Kenmochi K., Kimura R., Kobayashi M., Kuroita T., Kuwayama H., Maruyama Y., Matsuo K., Minami K., Mitsubori M., Mori M., Morishita R., Murase A., Nishikawa A., Nishikawa S., Okamoto T., Sakagami N., Sakamoto Y., Sasaki Y., Seki T., Sono S., Sugiyama A., Sumiya T., Takayama T., Takayama Y., Takeda H., Togashi T., Yahata K., Yamada H., Yanagisawa Y., Endo Y., Imamoto F., Kisu Y., Tanaka S., Isogai T., Imai J., Watanabe S., Nomura N. Nat. Methods 5:1011-1017(2008) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
[5]	"The DNA sequence and biological annotation of human chromosome 1." Gregory S.G., Barlow K.F., McLay K.E., Kaul R., Swarbreck D., Dunham A., Scott C.E., Howe K.L., Woodfine K., Spencer C.C.A., Jones M.C., Gillson C., Searle S., Zhou Y., Kokocinski F., McDonald L., Evans R., Phillips K. , Atkinson A., Cooper R., Jones C., Hall R.E., Andrews T.D., Lloyd C., Ainscough R., Almeida J.P., Ambrose K.D., Anderson F., Andrew R.W., Ashwell R.I.S., Aubin K., Babbage A.K., Bagguley C.L., Bailey J., Beasley H., Bethel G., Bird C.P., Bray-Allen S., Brown J.Y., Brown A.J., Buckley D., Burton J., Bye J., Carder C., Chapman J.C., Clark S.Y., Clarke G., Clee C., Cobley V., Collier R.E., Corby N., Coville G.J., Davies J., Deadman R., Dunn M., Earthrowl M., Ellington A.G., Errington H., Frankish A., Frankland J., French L., Garner P., Garnett J., Gay L., Ghori M.R.J., Gibson R., Gilby L.M., Gillett W., Glithero R.J., Grafham D.V., Griffiths C., Griffiths-Jones S., Grocock R., Hammond S., Harrison E.S.I., Hart E., Haugen E., Heath P.D., Holmes S., Holt K., Howden P.J., Hunt A.R., Hunt S.E., Hunter G., Isherwood J., James R., Johnson C., Johnson D., Joy A., Kay M., Kershaw J.K., Kibukawa M., Kimberley A.M., King A., Knights A.J., Lad H., Laird G., Lawlor S., Leongamornlert D.A., Lloyd D.M., Loveland J., Lovell J., Lush M.J., Lyne R., Martin S., Mashreghi-Mohammadi M., Matthews L., Matthews N.S.W., McLaren S., Milne S., Mistry S., Moore M.J.F., Nickerson T., O'Dell C.N., Oliver K., Palmeiri A., Palmer S.A., Parker A., Patel D., Pearce A.V., Peck A.I., Pelan S., Phelps K., Phillimore B.J., Plumb R., Rajan J., Raymond C., Rouse G., Saenphimmachak C., Sehra H.K., Sheridan E., Shownkeen R., Sims S., Skuce C.D., Smith M., Steward C., Subramanian S., Sycamore N., Tracey A., Tromans A., Van Helmond Z., Wall M., Wallis J.M., White S., Whitehead S.L., Wilkinson J.E., Willey D.L., Williams H., Wilming L., Wray P.W., Wu Z., Coulson A., Vaudin M., Sulston J.E., Durbin R.M., Hubbard T., Wooster R., Dunham I., Carter N.P., McVean G., Ross M.T., Harrow J., Olson M.V., Beck S., Rogers J., Bentley D.R. Nature 441:315-321(2006) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[6]	"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)." The MGC Project Team Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. Tissue: Prostate.
[7]	"Members of the steroid hormone receptor superfamily interact with TFIIB (S300-II)." Ing N.H., Beekman J.M., Tsai S.Y., Tsai M.J., O'Malley B.W. J. Biol. Chem. 267:17617-17623(1992) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 6-316.
[8]	"Isolation and characterization of a cDNA encoding a new type of human transcription elongation factor S-II." Umehara T., Kida S., Yamamoto T., Horikoshi M. Gene 167:297-302(1995) [PubMed] [Europe PMC] [Abstract] Cited for: INTERACTION WITH TCEA2.
[9]	"The Epstein-Barr virus nuclear protein 2 acidic domain can interact with TFIIB, TAF40, and RPA70 but not with TATA-binding protein." Tong X., Wang F., Thut C.J., Kieff E. J. Virol. 69:585-588(1995) [PubMed] [Europe PMC] [Abstract] Cited for: INTERACTION WITH EBV EBNA2.
[10]	"The human immunodeficiency virus type 1 Vpr transactivator: cooperation with promoter-bound activator domains and binding to TFIIB." Agostini I., Navarro J.-M., Rey F., Bouhamdan M., Spire B., Vigne R., Sire J. J. Mol. Biol. 261:599-606(1996) [PubMed] [Europe PMC] [Abstract] Cited for: INTERACTION WITH HIV-1 VPR.
[11]	"The HIV-1 Vpr co-activator induces a conformational change in TFIIB." Agostini I., Navarro J.M., Bouhamdan M., Willetts K., Rey F., Spire B., Vigne R., Pomerantz R., Sire J. FEBS Lett. 450:235-239(1999) [PubMed] [Europe PMC] [Abstract] Cited for: MUTAGENESIS OF 52-GLU--SER-56.
[12]	"A quantitative atlas of mitotic phosphorylation." Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E., Elledge S.J., Gygi S.P. Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008) [PubMed] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-76, MASS SPECTROMETRY. Tissue: Cervix carcinoma.
[13]	"Quantitative phosphoproteomic analysis of T cell receptor signaling reveals system-wide modulation of protein-protein interactions." Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K., Rodionov V., Han D.K. Sci. Signal. 2:RA46-RA46(2009) [PubMed] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-76, MASS SPECTROMETRY. Tissue: Leukemic T-cell.
[14]	"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] [Europe PMC] [Abstract] Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[15]	"Solution structure of the C-terminal core domain of human TFIIB: similarity to cyclin A and interaction with TATA-binding protein." Bagby S., Kim S., Maldonado E., Tong K.I., Reinberg D., Ikura M. Cell 82:857-867(1995) [PubMed] [Europe PMC] [Abstract] Cited for: STRUCTURE BY NMR OF 111-316.
[16]	"Crystal structure of a TFIIB-TBP-TATA-element ternary complex." Nikolov D.B., Chen H., Halay E.D., Usheva A.A., Hisatake K., Lee D.K., Roeder R.G., Burley S.K. Nature 377:119-128(1995) [PubMed] [Europe PMC] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (2.7 ANGSTROMS) OF 112-316.
[17]	"Structure of a (Cys3His) zinc ribbon, a ubiquitous motif in archaeal and eucaryal transcription." Chen H.T., Legault P., Glushka J., Omichinski J.G., Scott R.A. Protein Sci. 9:1743-1752(2000) [PubMed] [Europe PMC] [Abstract] Cited for: STRUCTURE BY NMR OF 2-59.
[18]	"The consensus coding sequences of human breast and colorectal cancers." Sjoeblom T., Jones S., Wood L.D., Parsons D.W., Lin J., Barber T.D., Mandelker D., Leary R.J., Ptak J., Silliman N., Szabo S., Buckhaults P., Farrell C., Meeh P., Markowitz S.D., Willis J., Dawson D., Willson J.K.V. , Gazdar A.F., Hartigan J., Wu L., Liu C., Parmigiani G., Park B.H., Bachman K.E., Papadopoulos N., Vogelstein B., Kinzler K.W., Velculescu V.E. Science 314:268-274(2006) [PubMed] [Europe PMC] [Abstract] Cited for: VARIANT [LARGE SCALE ANALYSIS] GLN-132.
+	Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ

X59268 mRNA. Translation: CAA41958.1.
M76766 mRNA. Translation: AAA61149.1.
AK289822 mRNA. Translation: BAF82511.1.
AB451296 mRNA. Translation: BAG70110.1.
AL445991 Genomic DNA. Translation: CAI41341.1.
BC020597 mRNA. Translation: AAH20597.1.
S44184 mRNA. Translation: AAB23144.1.

IPI

IPI00022820.

PIR

TWHU2B. S17654.

RefSeq

NP_001505.1. NM_001514.5.

UniGene

Hs.481852.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
1C9B	X-ray	2.65	A/E/I/M/Q	110-316	[»]
1DL6	NMR	-	A	2-59	[»]
1RLY	NMR	-	A	1-60	[»]
1RO4	NMR	-	A	1-60	[»]
1TFB	NMR	-	A	112-316	[»]
1VOL	X-ray	2.70	A	113-316	[»]
2PHG	NMR	-	A	112-316	[»]

ProteinModelPortal

Q00403.

ModBase

Search...

Protein-protein interaction databases

DIP

DIP-1077N.

IntAct

Q00403. 20 interactions.

MINT

MINT-156550.

STRING

9606.ENSP00000359531.

PTM databases

PhosphoSite

Q00403.

Polymorphism databases

DMDM

135629.

Proteomic databases

PaxDb

Q00403.

PeptideAtlas

Q00403.

PRIDE

Q00403.

Protocols and materials databases

DNASU

2959.

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

Ensembl

ENST00000370500; ENSP00000359531; ENSG00000137947.

GeneID

2959.

KEGG

hsa:2959.

UCSC

uc001dmo.4. human.

Organism-specific databases

CTD

2959.

GeneCards

GC01M089318.

HGNC

HGNC:4648. GTF2B.

MIM

189963. gene.

neXtProt

NX_Q00403.

PharmGKB

PA29035.

GenAtlas

Search...

Phylogenomic databases

eggNOG

COG1405.

HOGENOM

HOG000108634.

HOVERGEN

HBG017914.

InParanoid

Q00403.

KO

K03124.

OMA

WRAFDPD.

OrthoDB

EOG4QRH4F.

PhylomeDB

Q00403.

Enzyme and pathway databases

Reactome

REACT_116125. Disease.
REACT_1788. Transcription.
REACT_71. Gene Expression.

Gene expression databases

ArrayExpress

Q00403.

Bgee

Q00403.

CleanEx

HS_GTF2B.

Genevestigator

Q00403.

GermOnline

ENSG00000137947. Homo sapiens.

Family and domain databases

Gene3D

1.10.472.10. 2 hits.

InterPro

IPR013763. Cyclin-like.
IPR000812. TFIIB.
IPR023486. TFIIB_CS.
IPR013150. TFIIB_cyclin.
IPR013137. Znf_TFIIB.
[Graphical view]

PANTHER

PTHR11618. PTHR11618. 1 hit.

Pfam

PF08271. TF_Zn_Ribbon. 1 hit.
PF00382. TFIIB. 2 hits.
[Graphical view]

PRINTS

PR00685. TIFACTORIIB.

SMART

SM00385. CYCLIN. 2 hits.
[Graphical view]

SUPFAM

SSF47954. Cyclin_like. 2 hits.

PROSITE

PS00782. TFIIB. 2 hits.
PS51134. ZF_TFIIB. 1 hit.
[Graphical view]

ProtoNet

Search...

Other

ChiTaRS

GTF2B. human.

EvolutionaryTrace

Q00403.

GenomeRNAi

2959.

NextBio

11730.

PMAP-CutDB

Q00403.

SOURCE

Search...

Entry information

Entry name

TF2B_HUMAN

Accession

Primary (citable) accession number: Q00403
Secondary accession number(s): A8K1A7, Q5JS30

Entry history

Integrated into UniProtKB/Swiss-Prot:	December 1, 1992
Last sequence update:	December 1, 1992
Last modified:	May 1, 2013
This is version 148 of the entry and version 1 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.