P13984 (T2FB_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
General transcription factor IIF subunit 2
EC=3.6.4.12

Alternative name(s):
ATP-dependent helicase GTF2F2
General transcription factor IIF 30 kDa subunit
Transcription initiation factor IIF subunit beta
Short name=TFIIF-beta
Transcription initiation factor RAP30

Gene names

Name:	GTF2F2
Synonyms:	RAP30

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 › Dipnotetrapodomorpha › Tetrapoda › Amniota › Mammalia › Theria › Eutheria › Boreoeutheria › Euarchontoglires › Primates › Haplorrhini › Simiiformes › Catarrhini › Hominoidea › Hominidae › Homininae › Homo

Protein attributes

Sequence length	249 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	TFIIF is a general transcription initiation factor that binds to RNA polymerase II and helps to recruit it to the initiation complex in collaboration with TFIIB. It promotes transcription elongation. This subunit shows ATP-dependent DNA-helicase activity. Ref.1
Catalytic activity	ATP + H2O = ADP + phosphate.
Subunit structure	Heterodimer of an alpha and a beta subunit. Interacts with HTATSF1 and GPBP1 By similarity. Interacts with URI1. Ref.8 Ref.9
Subcellular location	Nucleus Ref.8.
Sequence similarities	Belongs to the TFIIF beta subunit family.

Ontologies

Keywords
Biological process	Transcription Transcription regulation
Cellular component	Nucleus
Ligand	ATP-binding DNA-binding Nucleotide-binding
Molecular function	Helicase Hydrolase
PTM	Acetylation Phosphoprotein
Technical term	3D-structure Complete proteome Direct protein sequencing Reference proteome
Gene Ontology (GO)
Biological_process	7-methylguanosine mRNA capping Traceable author statement. Source: Reactome RNA splicing Traceable author statement. Source: Reactome gene expression Traceable author statement. Source: Reactome mRNA splicing, via spliceosome Traceable author statement. Source: Reactome positive regulation of viral transcription Traceable author statement. Source: Reactome regulation of transcription, DNA-templated Inferred from electronic annotation. Source: UniProtKB-KW transcription elongation from RNA polymerase II promoter Traceable author statement. Source: Reactome transcription from RNA polymerase II promoter Traceable author statement. Source: Reactome transcription initiation from RNA polymerase II promoter Traceable author statement. Source: Reactome viral process Traceable author statement. Source: Reactome
Cellular_component	microtubule cytoskeleton Inferred from direct assay. Source: HPA nucleoplasm Traceable author statement. Source: Reactome nucleus Inferred from direct assay. Source: HPA transcription factor TFIIF complex Inferred from electronic annotation. Source: InterPro
Molecular_function	ATP binding Inferred from electronic annotation. Source: UniProtKB-KW ATP-dependent helicase activity Inferred from electronic annotation. Source: InterPro DNA binding Inferred from electronic annotation. Source: UniProtKB-KW protein binding Inferred from physical interaction Ref.9. Source: UniProtKB
Complete GO annotation...

Binary interactions

With	Entry	#Exp.	IntAct	Notes
RPL27A	P46776	2	EBI-1030560,EBI-350581
TCTEX1D2	Q8WW35	2	EBI-1030560,EBI-2692044
URI1	O94763	4	EBI-1030560,EBI-357067

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Initiator methionine

1

1

Removed Ref.11

Chain

2 – 249

248

General transcription factor IIF subunit 2

PRO_0000211235

Regions

Nucleotide binding

36 – 43

8

ATP Potential

Amino acid modifications

Modified residue

2

1

N-acetylalanine Ref.11

Modified residue

22

1

N6-acetyllysine Ref.12

Modified residue

33

1

N6-acetyllysine Ref.12

Modified residue

137

1

N6-acetyllysine Ref.12

Modified residue

142

1

Phosphoserine Ref.10

Modified residue

248

1

Phosphoserine Ref.13

Secondary structure

1

.

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.

.

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.

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249

Helix Strand Turn

Details...

Beta strand

6 – 8

3

Helix

10 – 13

4

Beta strand

17 – 24

8

Helix

25 – 31

7

Beta strand

39 – 48

10

Beta strand

51 – 58

8

Helix

60 – 63

4

Beta strand

80 – 86

7

Beta strand

91 – 99

9

Beta strand

104 – 116

13

Helix

177 – 193

17

Helix

199 – 205

7

Helix

210 – 220

11

Sequences

	Sequence		Length	Mass (Da)
	P13984 [UniParc]. Last modified February 1, 1994. Version 2. Checksum: 05A1A9F8D31B749C	FASTA	249	28,380
	10 20 30 40 50 60 MAERGELDLT GAKQNTGVWL VKVPKYLSQQ WAKASGRGEV GKLRIAKTQG RTEVSFTLNE 70 80 90 100 110 120 DLANIHDIGG KPASVSAPRE HPFVLQSVGG QTLTVFTESS SDKLSLEGIV VQRAECRPAA 130 140 150 160 170 180 SENYMRLKRL QIEESSKPVR LSQQLDKVVT TNYKPVANHQ YNIEYERKKK EDGKRARADK 190 200 210 220 230 240 QHVLDMLFSA FEKHQYYNLK DLVDITKQPV VYLKEILKEI GVQNVKGIHK NTWELKPEYR HYQGEEKSD

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Structure and associated DNA-helicase activity of a general transcription initiation factor that binds to RNA polymerase II." Sopta M., Burton Z.F., Greenblatt J. Nature 341:410-414(1989) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA], PARTIAL PROTEIN SEQUENCE, FUNCTION. Tissue: Kidney.
[2]	"Nucleotide and amino acid sequence of RAP30." Horikoshi M., Fujita H., Wang J., Takada R., Roeder R.G. Nucleic Acids Res. 19:5436-5436(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: Placenta.
[4]	"Cloning of human full-length CDSs in BD Creator(TM) system donor vector." Kalnine N., Chen X., Rolfs A., Halleck A., Hines L., Eisenstein S., Koundinya M., Raphael J., Moreira D., Kelley T., LaBaer J., Lin Y., Phelan M., Farmer A. Submitted (OCT-2004) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
[5]	"The DNA sequence and analysis of human chromosome 13." Dunham A., Matthews L.H., Burton J., Ashurst J.L., Howe K.L., Ashcroft K.J., Beare D.M., Burford D.C., Hunt S.E., Griffiths-Jones S., Jones M.C., Keenan S.J., Oliver K., Scott C.E., Ainscough R., Almeida J.P., Ambrose K.D., Andrews D.T. , Ashwell R.I.S., Babbage A.K., Bagguley C.L., Bailey J., Bannerjee R., Barlow K.F., Bates K., Beasley H., Bird C.P., Bray-Allen S., Brown A.J., Brown J.Y., Burrill W., Carder C., Carter N.P., Chapman J.C., Clamp M.E., Clark S.Y., Clarke G., Clee C.M., Clegg S.C., Cobley V., Collins J.E., Corby N., Coville G.J., Deloukas P., Dhami P., Dunham I., Dunn M., Earthrowl M.E., Ellington A.G., Faulkner L., Frankish A.G., Frankland J., French L., Garner P., Garnett J., Gilbert J.G.R., Gilson C.J., Ghori J., Grafham D.V., Gribble S.M., Griffiths C., Hall R.E., Hammond S., Harley J.L., Hart E.A., Heath P.D., Howden P.J., Huckle E.J., Hunt P.J., Hunt A.R., Johnson C., Johnson D., Kay M., Kimberley A.M., King A., Laird G.K., Langford C.J., Lawlor S., Leongamornlert D.A., Lloyd D.M., Lloyd C., Loveland J.E., Lovell J., Martin S., Mashreghi-Mohammadi M., McLaren S.J., McMurray A., Milne S., Moore M.J.F., Nickerson T., Palmer S.A., Pearce A.V., Peck A.I., Pelan S., Phillimore B., Porter K.M., Rice C.M., Searle S., Sehra H.K., Shownkeen R., Skuce C.D., Smith M., Steward C.A., Sycamore N., Tester J., Thomas D.W., Tracey A., Tromans A., Tubby B., Wall M., Wallis J.M., West A.P., Whitehead S.L., Willey D.L., Wilming L., Wray P.W., Wright M.W., Young L., Coulson A., Durbin R.M., Hubbard T., Sulston J.E., Beck S., Bentley D.R., Rogers J., Ross M.T. Nature 428:522-528(2004) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[6]	Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S., Turner R. , Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W., Venter J.C. Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[7]	"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: Eye.
[8]	"Tat-SF1 protein associates with RAP30 and human SPT5 proteins." Kim J.B., Yamaguchi Y., Wada T., Handa H., Sharp P.A. Mol. Cell. Biol. 19:5960-5968(1999) [PubMed] [Europe PMC] [Abstract] Cited for: INTERACTION WITH HTATSF1, SUBCELLULAR LOCATION.
[9]	"Interaction with general transcription factor IIF (TFIIF) is required for the suppression of activated transcription by RPB5-mediating protein (RMP)." Wei W., Gu J.X., Zhu C.Q., Sun F.Y., Dorjsuren D., Lin Y., Murakami S. Cell Res. 13:111-120(2003) [PubMed] [Europe PMC] [Abstract] Cited for: INTERACTION WITH URI1.
[10]	"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-142, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. Tissue: Cervix carcinoma.
[11]	"Lys-N and trypsin cover complementary parts of the phosphoproteome in a refined SCX-based approach." Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S. Anal. Chem. 81:4493-4501(2009) [PubMed] [Europe PMC] [Abstract] Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS], CLEAVAGE OF INITIATOR METHIONINE [LARGE SCALE ANALYSIS].
[12]	"Lysine acetylation targets protein complexes and co-regulates major cellular functions." Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T.C., Olsen J.V., Mann M. Science 325:834-840(2009) [PubMed] [Europe PMC] [Abstract] Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-22; LYS-33 AND LYS-137, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[13]	"Quantitative phosphoproteomics reveals widespread full phosphorylation site occupancy during mitosis." Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L., Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M. Sci. Signal. 3:RA3-RA3(2010) [PubMed] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-248, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. Tissue: Cervix carcinoma.
[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]	"Structural homology between the Rap30 DNA-binding domain and linker histone H5: implications for preinitiation complex assembly." Groft C.M., Uljon S.N., Wang R., Werner M.H. Proc. Natl. Acad. Sci. U.S.A. 95:9117-9122(1998) [PubMed] [Europe PMC] [Abstract] Cited for: STRUCTURE BY NMR OF 175-243.
+	Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ

X16901 mRNA. Translation: CAA34775.1.
X59745 mRNA. Translation: CAA42419.1.
AK291545 mRNA. Translation: BAF84234.1.
BT019525 mRNA. Translation: AAV38332.1.
AL138963, AL138693 Genomic DNA. Translation: CAH72032.1.
AL138693, AL138963 Genomic DNA. Translation: CAH72459.1.
CH471075 Genomic DNA. Translation: EAX08728.1.
BC001771 mRNA. Translation: AAH01771.1.

CCDS

CCDS9395.1.

PIR

S06141.
S18677.

RefSeq

NP_004119.1. NM_004128.2.

UniGene

Hs.654582.

3D structure databases

PDBe
RCSB-PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
1BBY	NMR	-	A	175-243	[»]
1F3U	X-ray	1.70	A/C/E/G	2-119	[»]
2BBY	NMR	-	A	175-243	[»]

ProteinModelPortal

P13984.

SMR

P13984. Positions 2-119, 175-243.

ModBase

Search...

MobiDB

Search...

Protein-protein interaction databases

BioGrid

109218. 39 interactions.

DIP

DIP-41680N.

IntAct

P13984. 31 interactions.

MINT

MINT-193667.

STRING

9606.ENSP00000340823.

PTM databases

PhosphoSite

P13984.

Polymorphism databases

DMDM

464519.

Proteomic databases

MaxQB

P13984.

PaxDb

P13984.

PeptideAtlas

P13984.

PRIDE

P13984.

Protocols and materials databases

DNASU

2963.

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

Ensembl

ENST00000340473; ENSP00000340823; ENSG00000188342.

GeneID

2963.

KEGG

hsa:2963.

UCSC

uc001uzw.3. human.

Organism-specific databases

CTD

2963.

GeneCards

GC13P045694.

HGNC

HGNC:4653. GTF2F2.

HPA

HPA006912.

MIM

189969. gene.

neXtProt

NX_P13984.

PharmGKB

PA29039.

GenAtlas

Search...

Phylogenomic databases

eggNOG

COG5090.

HOGENOM

HOG000294179.

HOVERGEN

HBG001606.

InParanoid

P13984.

KO

K03139.

OMA

WELKKEY.

OrthoDB

EOG7WX094.

PhylomeDB

P13984.

TreeFam

TF314290.

Enzyme and pathway databases

Reactome

REACT_116125. Disease.
REACT_1788. Transcription.
REACT_1892. Elongation arrest and recovery.
REACT_71. Gene Expression.

Gene expression databases

Bgee

P13984.

CleanEx

HS_GTF2F2.

Genevestigator

P13984.

Family and domain databases

Gene3D

1.10.10.10. 1 hit.

InterPro

IPR016640. TFIIF-beta_subgr.
IPR003196. TFIIF_beta.
IPR011039. TFIIF_interaction.
IPR011991. WHTH_DNA-bd_dom.
[Graphical view]

PANTHER

PTHR10445. PTHR10445. 1 hit.

Pfam

PF02270. TFIIF_beta. 2 hits.
[Graphical view]

PIRSF

PIRSF015849. TFIIF-beta. 1 hit.

SUPFAM

SSF50916. SSF50916. 1 hit.

ProtoNet

Search...

Other

EvolutionaryTrace

P13984.

GeneWiki

GTF2F2.

GenomeRNAi

2963.

NextBio

11746.

PRO

P13984.

SOURCE

Search...

Entry information

Entry name

T2FB_HUMAN

Accession

Primary (citable) accession number: P13984
Secondary accession number(s): A6NNS5, Q5W0H3

Entry history

Integrated into UniProtKB/Swiss-Prot:	January 1, 1990
Last sequence update:	February 1, 1994
Last modified:	July 9, 2014
This is version 152 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.