Reviewed, UniProtKB/Swiss-Prot Q00403 (TF2B_HUMAN)

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) [Complete proteome]

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

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

Protein attributes

Sequence length	316 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is not processed.
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.
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
Gene Ontology (GO)
Biological process	RNA elongation from RNA polymerase II promoter Inferred from Experiment. Source: Reactome interspecies interaction between organisms Inferred from electronic annotation. Source: UniProtKB-KW regulation of transcription, DNA-dependent Inferred from electronic annotation. Source: InterPro transcription initiation from RNA polymerase II promoter Inferred from Experiment. Source: Reactome translational initiation Inferred from electronic annotation. Source: InterPro
Cellular component	nucleoplasm Inferred from Experiment. Source: Reactome
Molecular function	general RNA polymerase II transcription factor activity Ref.15 Traceable author statement. Source: ProtInc protein binding Inferred from physical interaction. Source: UniProtKB translation initiation factor activity Inferred from electronic annotation. Source: InterPro zinc ion binding Inferred from electronic annotation. Source: UniProtKB-KW
Complete GO annotation...

Binary interactions

With	Entry	#Exp.	IntAct	Notes
GRF1	P42643	1	EBI-389564,EBI-876602	From a different organism.
GRF1	P49106	1	EBI-389564,EBI-2320214	From a different organism.
GRF2	Q01525	1	EBI-389564,EBI-637502	From a different organism.
GRF3	P42644	1	EBI-389564,EBI-2320234	From a different organism.
GRF4	P46077	2	EBI-389564,EBI-637479	From a different organism.
GRF7	Q96300	1	EBI-389564,EBI-637457	From a different organism.
POU3F2	P20265	1	EBI-389564,EBI-1167176
YWHAE	P62258	1	EBI-389564,EBI-356498

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

Natural variations

Natural variant

19

1

P → S: dbSNP rs1804499.

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

19 – 21

3

Beta strand

24 – 33

10

Turn

35 – 37

3

Helix

111 – 113

3

Helix

114 – 127

14

Helix

132 – 148

17

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

Sequences

	Sequence		Length	Mass (Da)
	Q00403-1 [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: 1876184] [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: 1946368] [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: 14702039] [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: 19054851] [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: 16710414] [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: 15489334] [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: 1517211] [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: 8566795] [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: 7983760] [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: 8800208] [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: 10359081] [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: 18669648] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-76, MASS SPECTROMETRY.
[13]	Colinge J., Superti-Furga G., Bennett K.L. Submitted (OCT-2008) to UniProtKB Cited for: IDENTIFICATION [LARGE SCALE ANALYSIS], MASS SPECTROMETRY.
[14]	"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: 19690332] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-76, MASS SPECTROMETRY. Tissue: T-cell.
[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: 7671313] [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: 7675079] [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: 11045620] [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: 16959974] [Abstract] Cited for: VARIANT [LARGE SCALE ANALYSIS] GLN-132.
+	Additional computationally mapped references.

Cross-references

Sequence databases

EMBLGenBankDDBJ

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.

UniGene

Hs.481852

3D structure databases

PDBPDBe

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	[»]

ModBase

Search...

Protein-protein interaction databases

DIP

DIP:1077N.

IntAct

Q00403. 10 interactions.

STRING

Q00403.

PTM databases

PhosphoSite

Q00403.

Proteomic databases

PeptideAtlas

Q00403.

PRIDE

Q00403.

Genome annotation databases

Ensembl

ENST00000370500; ENSP00000359531; ENSG00000137947; Homo sapiens. [Genome view]

GeneID

2959.

KEGG

hsa:2959.

UCSC

uc001dmo.2. human.

Organism-specific databases

CTD

2959.

GeneCards

GC01M089030.

H-InvDB

HIX0000760.

HGNC

HGNC:4648. GTF2B.

MIM

189963. gene.

PharmGKB

PA29035.

GenAtlas

Search...

Phylogenomic databases

HOGENOM

Q00403.

HOVERGEN

Q00403.

OMA

RTFSNEK

Enzyme and pathway databases

Reactome

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

Gene expression databases

ArrayExpress

Q00403.

Bgee

Q00403.

CleanEx

HS_GTF2B.

Genevestigator

Q00403.

GermOnline

ENSG00000137947. Homo sapiens.

Family and domain databases

InterPro

IPR006670. Cyclin.
IPR011028. Cyclin-like.
IPR013763. Cyclin_related.
IPR000812. TFIIB-related.
IPR013150. TFIIB_cyclin.
IPR013137. Znf_TFIIB.
[Graphical view]

Gene3D

G3DSA:1.10.472.10. Cyclin_related. 2 hits.

PANTHER

PTHR11618. TFIIB_euk_relate. 1 hit.

Pfam

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

PRINTS

PR00685. TIFACTORIIB.

SMART

SM00385. CYCLIN. 2 hits.
[Graphical view]

PROSITE

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

ProtoNet

Search...

Other Resources

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:	November 24, 2009
This is version 112 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

HPI (Human Proteome Initiative)

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.