GTF2F2

Functionⁱ

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.1 Publication

Catalytic activityⁱ

ATP + H₂O = ADP + phosphate.

Regions

Feature key	Position(s)	Length	Description	Graphical view	Feature identifier	Actions
Nucleotide bindingⁱ	36 – 43	8	ATPSequence analysis

Enzyme and pathway databases

Reactomeⁱ	R-HSA-112382. Formation of RNA Pol II elongation complex. R-HSA-113418. Formation of the Early Elongation Complex. R-HSA-167152. Formation of HIV elongation complex in the absence of HIV Tat. R-HSA-167158. Formation of the HIV-1 Early Elongation Complex. R-HSA-167160. RNA Pol II CTD phosphorylation and interaction with CE. R-HSA-167161. HIV Transcription Initiation. R-HSA-167162. RNA Polymerase II HIV Promoter Escape. R-HSA-167172. Transcription of the HIV genome. R-HSA-167200. Formation of HIV-1 elongation complex containing HIV-1 Tat. R-HSA-167238. Pausing and recovery of Tat-mediated HIV elongation. R-HSA-167242. Abortive elongation of HIV-1 transcript in the absence of Tat. R-HSA-167243. Tat-mediated HIV elongation arrest and recovery. R-HSA-167246. Tat-mediated elongation of the HIV-1 transcript. R-HSA-167287. HIV elongation arrest and recovery. R-HSA-167290. Pausing and recovery of HIV elongation. R-HSA-168325. Viral Messenger RNA Synthesis. R-HSA-674695. RNA Polymerase II Pre-transcription Events. R-HSA-6796648. TP53 Regulates Transcription of DNA Repair Genes. R-HSA-6803529. FGFR2 alternative splicing. R-HSA-6807505. RNA polymerase II transcribes snRNA genes. R-HSA-72086. mRNA Capping. R-HSA-72163. mRNA Splicing - Major Pathway. R-HSA-72165. mRNA Splicing - Minor Pathway. R-HSA-72203. Processing of Capped Intron-Containing Pre-mRNA. R-HSA-73776. RNA Polymerase II Promoter Escape. R-HSA-73779. RNA Polymerase II Transcription Pre-Initiation And Promoter Opening. R-HSA-75953. RNA Polymerase II Transcription Initiation. R-HSA-75955. RNA Polymerase II Transcription Elongation. R-HSA-76042. RNA Polymerase II Transcription Initiation And Promoter Clearance. R-HSA-77075. RNA Pol II CTD phosphorylation and interaction with CE. R-HSA-8851708. Signaling by FGFR2 IIIa TM.

Reactomeⁱ

R-HSA-112382. Formation of RNA Pol II elongation complex.
R-HSA-113418. Formation of the Early Elongation Complex.
R-HSA-167152. Formation of HIV elongation complex in the absence of HIV Tat.
R-HSA-167158. Formation of the HIV-1 Early Elongation Complex.
R-HSA-167160. RNA Pol II CTD phosphorylation and interaction with CE.
R-HSA-167161. HIV Transcription Initiation.
R-HSA-167162. RNA Polymerase II HIV Promoter Escape.
R-HSA-167172. Transcription of the HIV genome.
R-HSA-167200. Formation of HIV-1 elongation complex containing HIV-1 Tat.
R-HSA-167238. Pausing and recovery of Tat-mediated HIV elongation.
R-HSA-167242. Abortive elongation of HIV-1 transcript in the absence of Tat.
R-HSA-167243. Tat-mediated HIV elongation arrest and recovery.
R-HSA-167246. Tat-mediated elongation of the HIV-1 transcript.
R-HSA-167287. HIV elongation arrest and recovery.
R-HSA-167290. Pausing and recovery of HIV elongation.
R-HSA-168325. Viral Messenger RNA Synthesis.
R-HSA-674695. RNA Polymerase II Pre-transcription Events.
R-HSA-6796648. TP53 Regulates Transcription of DNA Repair Genes.
R-HSA-6803529. FGFR2 alternative splicing.
R-HSA-6807505. RNA polymerase II transcribes snRNA genes.
R-HSA-72086. mRNA Capping.
R-HSA-72163. mRNA Splicing - Major Pathway.
R-HSA-72165. mRNA Splicing - Minor Pathway.
R-HSA-72203. Processing of Capped Intron-Containing Pre-mRNA.
R-HSA-73776. RNA Polymerase II Promoter Escape.
R-HSA-73779. RNA Polymerase II Transcription Pre-Initiation And Promoter Opening.
R-HSA-75953. RNA Polymerase II Transcription Initiation.
R-HSA-75955. RNA Polymerase II Transcription Elongation.
R-HSA-76042. RNA Polymerase II Transcription Initiation And Promoter Clearance.
R-HSA-77075. RNA Pol II CTD phosphorylation and interaction with CE.
R-HSA-8851708. Signaling by FGFR2 IIIa TM.

Names & Taxonomyⁱ

Protein namesⁱ	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 namesⁱ	Name:GTF2F2 Synonyms:RAP30
Organismⁱ	Homo sapiens (Human)
Taxonomic identifierⁱ	9606 [NCBI]
Taxonomic lineageⁱ	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
Proteomesⁱ	UP000005640 Componentⁱ: Chromosome 13

Organism-specific databases

HGNCⁱ	HGNC:4653. GTF2F2.

HGNCⁱ

HGNC:4653. GTF2F2.

Subcellular locationⁱ

Nucleus
1 Publication
Manual assertion based on experiment inⁱ
- Ref.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.

GO - Cellular componentⁱ

holo TFIIH complex Source: Ensembl
microtubule cytoskeleton Source: HPA
nucleoplasm Source: Reactome
nucleus
Source: UniProtKB
Inferred from direct assayⁱ
- 16791210
transcription factor TFIIF complex Source: GO_Central

Complete GO annotation...

Keywords - Cellular componentⁱ

Nucleus

Pathology & Biotechⁱ

Organism-specific databases

PharmGKBⁱ	PA29039.

PharmGKBⁱ

PA29039.

Polymorphism and mutation databases

BioMutaⁱ	GTF2F2.
DMDMⁱ	464519.

PTM / Processingⁱ

Molecule processing

Feature key	Position(s)	Length	Description	Graphical view	Feature identifier	Actions
Initiator methionineⁱ			RemovedCombined sources Manual assertion inferred from combination of experimental and computational evidenceⁱ Ref.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, CLEAVAGE OF INITIATOR METHIONINE [LARGE SCALE ANALYSIS], IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Chainⁱ	2 – 249	248	General transcription factor IIF subunit 2		PRO_0000211235	Add BLAST

Amino acid modifications

Feature key	Position(s)	Length	Description
Modified residueⁱ	2 – 2	1	N-acetylalanineCombined sources Manual assertion inferred from combination of experimental and computational evidenceⁱ Ref.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, CLEAVAGE OF INITIATOR METHIONINE [LARGE SCALE ANALYSIS], IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Modified residueⁱ	22 – 22	1	N6-acetyllysineCombined sources Manual assertion inferred from combination of experimental and computational evidenceⁱ Ref.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].
Modified residueⁱ	33 – 33	1	N6-acetyllysineCombined sources Manual assertion inferred from combination of experimental and computational evidenceⁱ Ref.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].
Modified residueⁱ	137 – 137	1	N6-acetyllysineCombined sources Manual assertion inferred from combination of experimental and computational evidenceⁱ Ref.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].
Modified residueⁱ	142 – 142	1	PhosphoserineCombined sources Manual assertion inferred from combination of experimental and computational evidenceⁱ Ref.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].
Modified residueⁱ	248 – 248	1	PhosphoserineCombined sources Manual assertion inferred from combination of experimental and computational evidenceⁱ Ref.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].

Keywords - PTMⁱ

Acetylation, Phosphoprotein

Proteomic databases

EPDⁱ	P13984.
MaxQBⁱ	P13984.
PaxDbⁱ	P13984.
PeptideAtlasⁱ	P13984.
PRIDEⁱ	P13984.

PTM databases

iPTMnetⁱ	P13984.
PhosphoSiteⁱ	P13984.

Expressionⁱ

Gene expression databases

Bgeeⁱ	ENSG00000188342.
CleanExⁱ	HS_GTF2F2.
ExpressionAtlasⁱ	P13984. baseline and differential.
Genevisibleⁱ	P13984. HS.

Organism-specific databases

HPAⁱ	HPA006912.

Interactionⁱ

Subunit structureⁱ

Heterodimer of an alpha and a beta subunit. Interacts with HTATSF1 and GPBP1 (By similarity). Interacts with URI1.By similarity2 Publications

Binary interactionsⁱ

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

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

Protein-protein interaction databases

BioGridⁱ	109218. 51 interactions.
DIPⁱ	DIP-41680N.
IntActⁱ	P13984. 38 interactions.
MINTⁱ	MINT-193667.
STRINGⁱ	9606.ENSP00000340823.

Structureⁱ

Secondary structure

1

249

Legend: HelixTurnBeta strand

Show more details

Feature key	Position(s)	Length	Description
Beta strandⁱ	6 – 8	3	Combined sources Manual assertion inferred from combination of experimental and computational evidenceⁱ PDB:1F3U
Helixⁱ	10 – 13	4	Combined sources Manual assertion inferred from combination of experimental and computational evidenceⁱ PDB:1F3U
Beta strandⁱ	17 – 24	8	Combined sources Manual assertion inferred from combination of experimental and computational evidenceⁱ PDB:1F3U
Helixⁱ	25 – 31	7	Combined sources Manual assertion inferred from combination of experimental and computational evidenceⁱ PDB:1F3U
Beta strandⁱ	39 – 48	10	Combined sources Manual assertion inferred from combination of experimental and computational evidenceⁱ PDB:1F3U
Beta strandⁱ	51 – 58	8	Combined sources Manual assertion inferred from combination of experimental and computational evidenceⁱ PDB:1F3U
Helixⁱ	60 – 63	4	Combined sources Manual assertion inferred from combination of experimental and computational evidenceⁱ PDB:1F3U
Beta strandⁱ	80 – 86	7	Combined sources Manual assertion inferred from combination of experimental and computational evidenceⁱ PDB:1F3U
Beta strandⁱ	91 – 99	9	Combined sources Manual assertion inferred from combination of experimental and computational evidenceⁱ PDB:1F3U
Beta strandⁱ	104 – 116	13	Combined sources Manual assertion inferred from combination of experimental and computational evidenceⁱ PDB:1F3U
Helixⁱ	177 – 193	17	Combined sources Manual assertion inferred from combination of experimental and computational evidenceⁱ PDB:1BBY
Helixⁱ	199 – 205	7	Combined sources Manual assertion inferred from combination of experimental and computational evidenceⁱ PDB:1BBY
Helixⁱ	210 – 220	11	Combined sources Manual assertion inferred from combination of experimental and computational evidenceⁱ PDB:1BBY

3D structure databases

Select the link destinations:
PDBeⁱ
RCSB PDBⁱ
PDBjⁱ

Links Updated

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	[»]
5IY6	electron microscopy	7.20	T	1-249	[»]
5IY7	electron microscopy	8.60	T	1-249	[»]
5IY8	electron microscopy	7.90	T	1-249	[»]
5IY9	electron microscopy	6.30	T	1-249	[»]
5IYA	electron microscopy	5.40	T	1-249	[»]
5IYB	electron microscopy	3.90	T	1-249	[»]
5IYC	electron microscopy	3.90	T	1-249	[»]
5IYD	electron microscopy	3.90	T	1-249	[»]

ProteinModelPortalⁱ

P13984.

SMRⁱ

P13984. Positions 2-119, 175-243.

ModBaseⁱ

Search...

MobiDBⁱ

Search...

Miscellaneous databases

EvolutionaryTraceⁱ	P13984.

EvolutionaryTraceⁱ

P13984.

Family & Domainsⁱ

Sequence similaritiesⁱ

Belongs to the TFIIF beta subunit family.Curated

Phylogenomic databases

eggNOGⁱ	KOG2905. Eukaryota. COG5090. LUCA.
GeneTreeⁱ	ENSGT00390000016051.
HOGENOMⁱ	HOG000294179.
HOVERGENⁱ	HBG001606.
InParanoidⁱ	P13984.
KOⁱ	K03139.
OMAⁱ	IANKWEK.
OrthoDBⁱ	EOG091G0IN2.
PhylomeDBⁱ	P13984.
TreeFamⁱ	TF314290.

Family and domain databases

Gene3Dⁱ	1.10.10.10. 1 hit.
InterProⁱ	IPR003196. TFIIF_beta. IPR011039. TFIIF_interaction. IPR011991. WHTH_DNA-bd_dom. [Graphical view]
PANTHERⁱ	PTHR10445. PTHR10445. 1 hit.
Pfamⁱ	PF02270. TFIIF_beta. 1 hit. [Graphical view]
PIRSFⁱ	PIRSF015849. TFIIF-beta. 1 hit.
SUPFAMⁱ	SSF46785. SSF46785. 1 hit. SSF50916. SSF50916. 1 hit.

Sequenceⁱ

Sequence statusⁱ: Complete.

Sequence processingⁱ: The displayed sequence is further processed into a mature form.

P13984-1 [UniParc]FASTA Add to basket

« Hide

        10         20         30         40         50
MAERGELDLT GAKQNTGVWL VKVPKYLSQQ WAKASGRGEV GKLRIAKTQG 
        60         70         80         90        100
RTEVSFTLNE DLANIHDIGG KPASVSAPRE HPFVLQSVGG QTLTVFTESS 
       110        120        130        140        150
SDKLSLEGIV VQRAECRPAA SENYMRLKRL QIEESSKPVR LSQQLDKVVT 
       160        170        180        190        200
TNYKPVANHQ YNIEYERKKK EDGKRARADK QHVLDMLFSA FEKHQYYNLK 
       210        220        230        240 
DLVDITKQPV VYLKEILKEI GVQNVKGIHK NTWELKPEYR HYQGEEKSD

Length:249

Mass (Da):28,380

Last modified:February 1, 1994 - v2

Checksum:ⁱ05A1A9F8D31B749C

GO

Sequence databases

Select the link destinations: EMBLⁱ GenBankⁱ DDBJⁱ Links Updated	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.
CCDSⁱ	CCDS9395.1.
PIRⁱ	S06141. S18677.
RefSeqⁱ	NP_004119.1. NM_004128.2.
UniGeneⁱ	Hs.654582.

Genome annotation databases

Ensemblⁱ	ENST00000340473; ENSP00000340823; ENSG00000188342.
GeneIDⁱ	2963.
KEGGⁱ	hsa:2963.
UCSCⁱ	uc001uzw.4. human.

Cross-referencesⁱ

Sequence databases

Select the link destinations: EMBLⁱ GenBankⁱ DDBJⁱ Links Updated	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.
CCDSⁱ	CCDS9395.1.
PIRⁱ	S06141. S18677.
RefSeqⁱ	NP_004119.1. NM_004128.2.
UniGeneⁱ	Hs.654582.

3D structure databases

Select the link destinations:
PDBeⁱ
RCSB PDBⁱ
PDBjⁱ

Links Updated

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	[»]
5IY6	electron microscopy	7.20	T	1-249	[»]
5IY7	electron microscopy	8.60	T	1-249	[»]
5IY8	electron microscopy	7.90	T	1-249	[»]
5IY9	electron microscopy	6.30	T	1-249	[»]
5IYA	electron microscopy	5.40	T	1-249	[»]
5IYB	electron microscopy	3.90	T	1-249	[»]
5IYC	electron microscopy	3.90	T	1-249	[»]
5IYD	electron microscopy	3.90	T	1-249	[»]

ProteinModelPortalⁱ

P13984.

SMRⁱ

P13984. Positions 2-119, 175-243.

ModBaseⁱ

Search...

MobiDBⁱ

Search...

Protein-protein interaction databases

BioGridⁱ	109218. 51 interactions.
DIPⁱ	DIP-41680N.
IntActⁱ	P13984. 38 interactions.
MINTⁱ	MINT-193667.
STRINGⁱ	9606.ENSP00000340823.

PTM databases

iPTMnetⁱ	P13984.
PhosphoSiteⁱ	P13984.

Polymorphism and mutation databases

BioMutaⁱ	GTF2F2.
DMDMⁱ	464519.

Proteomic databases

EPDⁱ	P13984.
MaxQBⁱ	P13984.
PaxDbⁱ	P13984.
PeptideAtlasⁱ	P13984.
PRIDEⁱ	P13984.

Protocols and materials databases

DNASUⁱ	2963.
Structural Biology Knowledgebase	Search...

Genome annotation databases

Ensemblⁱ	ENST00000340473; ENSP00000340823; ENSG00000188342.
GeneIDⁱ	2963.
KEGGⁱ	hsa:2963.
UCSCⁱ	uc001uzw.4. human.

Organism-specific databases

CTDⁱ	2963.
GeneCardsⁱ	GTF2F2.
HGNCⁱ	HGNC:4653. GTF2F2.
HPAⁱ	HPA006912.
MIMⁱ	189969. gene.
neXtProtⁱ	NX_P13984.
PharmGKBⁱ	PA29039.
GenAtlasⁱ	Search...

Phylogenomic databases

eggNOGⁱ	KOG2905. Eukaryota. COG5090. LUCA.
GeneTreeⁱ	ENSGT00390000016051.
HOGENOMⁱ	HOG000294179.
HOVERGENⁱ	HBG001606.
InParanoidⁱ	P13984.
KOⁱ	K03139.
OMAⁱ	IANKWEK.
OrthoDBⁱ	EOG091G0IN2.
PhylomeDBⁱ	P13984.
TreeFamⁱ	TF314290.

Enzyme and pathway databases

Reactomeⁱ	R-HSA-112382. Formation of RNA Pol II elongation complex. R-HSA-113418. Formation of the Early Elongation Complex. R-HSA-167152. Formation of HIV elongation complex in the absence of HIV Tat. R-HSA-167158. Formation of the HIV-1 Early Elongation Complex. R-HSA-167160. RNA Pol II CTD phosphorylation and interaction with CE. R-HSA-167161. HIV Transcription Initiation. R-HSA-167162. RNA Polymerase II HIV Promoter Escape. R-HSA-167172. Transcription of the HIV genome. R-HSA-167200. Formation of HIV-1 elongation complex containing HIV-1 Tat. R-HSA-167238. Pausing and recovery of Tat-mediated HIV elongation. R-HSA-167242. Abortive elongation of HIV-1 transcript in the absence of Tat. R-HSA-167243. Tat-mediated HIV elongation arrest and recovery. R-HSA-167246. Tat-mediated elongation of the HIV-1 transcript. R-HSA-167287. HIV elongation arrest and recovery. R-HSA-167290. Pausing and recovery of HIV elongation. R-HSA-168325. Viral Messenger RNA Synthesis. R-HSA-674695. RNA Polymerase II Pre-transcription Events. R-HSA-6796648. TP53 Regulates Transcription of DNA Repair Genes. R-HSA-6803529. FGFR2 alternative splicing. R-HSA-6807505. RNA polymerase II transcribes snRNA genes. R-HSA-72086. mRNA Capping. R-HSA-72163. mRNA Splicing - Major Pathway. R-HSA-72165. mRNA Splicing - Minor Pathway. R-HSA-72203. Processing of Capped Intron-Containing Pre-mRNA. R-HSA-73776. RNA Polymerase II Promoter Escape. R-HSA-73779. RNA Polymerase II Transcription Pre-Initiation And Promoter Opening. R-HSA-75953. RNA Polymerase II Transcription Initiation. R-HSA-75955. RNA Polymerase II Transcription Elongation. R-HSA-76042. RNA Polymerase II Transcription Initiation And Promoter Clearance. R-HSA-77075. RNA Pol II CTD phosphorylation and interaction with CE. R-HSA-8851708. Signaling by FGFR2 IIIa TM.

Reactomeⁱ

R-HSA-112382. Formation of RNA Pol II elongation complex.
R-HSA-113418. Formation of the Early Elongation Complex.
R-HSA-167152. Formation of HIV elongation complex in the absence of HIV Tat.
R-HSA-167158. Formation of the HIV-1 Early Elongation Complex.
R-HSA-167160. RNA Pol II CTD phosphorylation and interaction with CE.
R-HSA-167161. HIV Transcription Initiation.
R-HSA-167162. RNA Polymerase II HIV Promoter Escape.
R-HSA-167172. Transcription of the HIV genome.
R-HSA-167200. Formation of HIV-1 elongation complex containing HIV-1 Tat.
R-HSA-167238. Pausing and recovery of Tat-mediated HIV elongation.
R-HSA-167242. Abortive elongation of HIV-1 transcript in the absence of Tat.
R-HSA-167243. Tat-mediated HIV elongation arrest and recovery.
R-HSA-167246. Tat-mediated elongation of the HIV-1 transcript.
R-HSA-167287. HIV elongation arrest and recovery.
R-HSA-167290. Pausing and recovery of HIV elongation.
R-HSA-168325. Viral Messenger RNA Synthesis.
R-HSA-674695. RNA Polymerase II Pre-transcription Events.
R-HSA-6796648. TP53 Regulates Transcription of DNA Repair Genes.
R-HSA-6803529. FGFR2 alternative splicing.
R-HSA-6807505. RNA polymerase II transcribes snRNA genes.
R-HSA-72086. mRNA Capping.
R-HSA-72163. mRNA Splicing - Major Pathway.
R-HSA-72165. mRNA Splicing - Minor Pathway.
R-HSA-72203. Processing of Capped Intron-Containing Pre-mRNA.
R-HSA-73776. RNA Polymerase II Promoter Escape.
R-HSA-73779. RNA Polymerase II Transcription Pre-Initiation And Promoter Opening.
R-HSA-75953. RNA Polymerase II Transcription Initiation.
R-HSA-75955. RNA Polymerase II Transcription Elongation.
R-HSA-76042. RNA Polymerase II Transcription Initiation And Promoter Clearance.
R-HSA-77075. RNA Pol II CTD phosphorylation and interaction with CE.
R-HSA-8851708. Signaling by FGFR2 IIIa TM.

Miscellaneous databases

ChiTaRSⁱ	GTF2F2. human.
EvolutionaryTraceⁱ	P13984.
GeneWikiⁱ	GTF2F2.
GenomeRNAiⁱ	2963.
PROⁱ	P13984.
SOURCEⁱ	Search...

Gene expression databases

Bgeeⁱ	ENSG00000188342.
CleanExⁱ	HS_GTF2F2.
ExpressionAtlasⁱ	P13984. baseline and differential.
Genevisibleⁱ	P13984. HS.

Family and domain databases

Gene3Dⁱ	1.10.10.10. 1 hit.
InterProⁱ	IPR003196. TFIIF_beta. IPR011039. TFIIF_interaction. IPR011991. WHTH_DNA-bd_dom. [Graphical view]
PANTHERⁱ	PTHR10445. PTHR10445. 1 hit.
Pfamⁱ	PF02270. TFIIF_beta. 1 hit. [Graphical view]
PIRSFⁱ	PIRSF015849. TFIIF-beta. 1 hit.
SUPFAMⁱ	SSF46785. SSF46785. 1 hit. SSF50916. SSF50916. 1 hit.
ProtoNetⁱ	Search...

Entry informationⁱ

Entry nameⁱ

T2FB_HUMAN

Accessionⁱ

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

Entry historyⁱ

Integrated into UniProtKB/Swiss-Prot:	January 1, 1990
Last sequence update:	February 1, 1994
Last modified:	September 7, 2016
This is version 174 of the entry and version 2 of the sequence. [Complete history]

Entry statusⁱ

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.

Miscellaneousⁱ

Keywords - Technical termⁱ

3D-structure, Complete proteome, Direct protein sequencing, Reference proteome

Documents

Human chromosome 13
Human chromosome 13: entries, gene names and cross-references to MIM
MIM cross-references
Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
PDB cross-references
Index of Protein Data Bank (PDB) cross-references
SIMILARITY comments
Index of protein domains and families

Similar proteinsⁱ

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:

100%	UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%	UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%	UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.

UniProtKB

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UniRef

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Supporting data

UniProtKB - P13984 (T2FB_HUMAN)

UniProt

P13984 - T2FB_HUMAN

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General transcription factor IIF subunit 2

Select a section on the left to see content.

<p>Provides any useful information about the protein, mostly biological knowledge.</p><p><a href='../manual/function_section' target='_top'>More...</a></p>Functioni

Regions

<p>The <a href="http://www.geneontology.org/">Gene Ontology (GO)</a> project provides a set of hierarchical controlled vocabulary split into 3 categories:</p><p><a href='../manual/gene_ontology' target='_top'>More...</a></p>GO - Molecular functioni

<p>The <a href="http://www.geneontology.org/">Gene Ontology (GO)</a> project provides a set of hierarchical controlled vocabulary split into 3 categories:</p><p><a href='../manual/gene_ontology' target='_top'>More...</a></p>GO - Biological processi

Enzyme and pathway databases

<p>Provides information about the protein and gene name(s) and synonym(s) and about the organism that is the source of the protein sequence.</p><p><a href='../manual/names_and_taxonomy_section' target='_top'>More...</a></p>Names & Taxonomyi

Organism-specific databases

<p>Provides information on the location and the topology of the mature protein in the cell.</p><p><a href='../manual/subcellular_location_section' target='_top'>More...</a></p>Subcellular locationi

<p>The <a href="http://www.geneontology.org/">Gene Ontology (GO)</a> project provides a set of hierarchical controlled vocabulary split into 3 categories:</p><p><a href='../manual/gene_ontology' target='_top'>More...</a></p>GO - Cellular componenti

<p>Provides information on the disease(s) and phenotype(s) associated with a protein.</p><p><a href='../manual/pathology_and_biotech_section' target='_top'>More...</a></p>Pathology & Biotechi

Organism-specific databases

Polymorphism and mutation databases

<p>Describes post-translational modifications (PTMs) and/or processing events.</p><p><a href='../manual/ptm_processing_section' target='_top'>More...</a></p>PTM / Processingi

Molecule processing

Amino acid modifications

Proteomic databases

PTM databases

<p>Provides information on the expression of a gene at the mRNA or protein level in cells or in tissues of multicellular organisms.</p><p><a href='../manual/expression_section' target='_top'>More...</a></p>Expressioni

Gene expression databases

Organism-specific databases

<p>Provides information on the quaternary structure of a protein and on interaction(s) with other proteins or protein complexes.</p><p><a href='../manual/interaction_section' target='_top'>More...</a></p>Interactioni

Protein-protein interaction databases

<p>Provides information on the tertiary and secondary structure of a protein.</p><p><a href='../manual/structure_section' target='_top'>More...</a></p>Structurei

Secondary structure

3D structure databases

Miscellaneous databases

<p>Provides information on sequence similarities with other proteins and the domain(s) present in a protein.</p><p><a href='../manual/family_and_domains_section' target='_top'>More...</a></p>Family & Domainsi

<p>Provides information about the sequence similarity with other proteins.</p><p><a href='../manual/sequence_similarities' target='_top'>More...</a></p>Sequence similaritiesi

Phylogenomic databases

Family and domain databases

<p>Displays by default the canonical protein sequence and upon request all isoforms described in the entry. It also includes information pertinent to the sequence(s), including length and molecular weight.</p><p><a href='../manual/sequences_section' target='_top'>More...</a></p>Sequencei

Sequence databases

Genome annotation databases

<p>Is used to point to information related to entries and found in data collections other than UniProtKB.</p><p><a href='../manual/cross_references_section' target='_top'>More...</a></p>Cross-referencesi

Sequence databases

3D structure databases

Protein-protein interaction databases

PTM databases

Polymorphism and mutation databases

Proteomic databases

Protocols and materials databases

Genome annotation databases

Organism-specific databases

Phylogenomic databases

Enzyme and pathway databases

Miscellaneous databases

Gene expression databases

Family and domain databases

<p>Provides general information on the entry.</p><p><a href='../manual/entry_information_section' target='_top'>More...</a></p>Entry informationi

<p>Contains any relevant information that doesn’t fit in any other defined sections</p><p><a href='../manual/miscellaneous_section' target='_top'>More...</a></p>Miscellaneousi

Documents

Functionⁱ

GO - Molecular functionⁱ

GO - Biological processⁱ

Names & Taxonomyⁱ

Subcellular locationⁱ

GO - Cellular componentⁱ

Pathology & Biotechⁱ

PTM / Processingⁱ

Expressionⁱ

Interactionⁱ

Structureⁱ

Family & Domainsⁱ

Sequence similaritiesⁱ

Sequenceⁱ

Cross-referencesⁱ

Entry informationⁱ

Miscellaneousⁱ