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Protein

General transcription factor IIF subunit 2

Gene

GTF2F2

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

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 keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi36 – 438ATPSequence analysis

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Helicase, Hydrolase

Keywords - Biological processi

Transcription, Transcription regulation

Keywords - Ligandi

ATP-binding, DNA-binding, Nucleotide-binding

Enzyme and pathway databases

ReactomeiR-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
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
Proteomesi
  • UP000005640 Componenti: Chromosome 13

Organism-specific databases

HGNCiHGNC:4653. GTF2F2.

Subcellular locationi

  • Nucleus 1 Publication

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Nucleus

Pathology & Biotechi

Organism-specific databases

PharmGKBiPA29039.

Polymorphism and mutation databases

BioMutaiGTF2F2.
DMDMi464519.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methionineiRemovedCombined sources
Chaini2 – 249248General transcription factor IIF subunit 2PRO_0000211235Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei2 – 21N-acetylalanineCombined sources
Modified residuei22 – 221N6-acetyllysineCombined sources
Modified residuei33 – 331N6-acetyllysineCombined sources
Modified residuei137 – 1371N6-acetyllysineCombined sources
Modified residuei142 – 1421PhosphoserineCombined sources
Modified residuei248 – 2481PhosphoserineCombined sources

Keywords - PTMi

Acetylation, Phosphoprotein

Proteomic databases

EPDiP13984.
MaxQBiP13984.
PaxDbiP13984.
PeptideAtlasiP13984.
PRIDEiP13984.

PTM databases

iPTMnetiP13984.
PhosphoSiteiP13984.

Expressioni

Gene expression databases

BgeeiENSG00000188342.
CleanExiHS_GTF2F2.
ExpressionAtlasiP13984. baseline and differential.
GenevisibleiP13984. HS.

Organism-specific databases

HPAiHPA006912.

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

WithEntry#Exp.IntActNotes
RPL27AP467762EBI-1030560,EBI-350581
TCTEX1D2Q8WW352EBI-1030560,EBI-2692044
URI1O947634EBI-1030560,EBI-357067

Protein-protein interaction databases

BioGridi109218. 51 interactions.
DIPiDIP-41680N.
IntActiP13984. 38 interactions.
MINTiMINT-193667.
STRINGi9606.ENSP00000340823.

Structurei

Secondary structure

1
249
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi6 – 83Combined sources
Helixi10 – 134Combined sources
Beta strandi17 – 248Combined sources
Helixi25 – 317Combined sources
Beta strandi39 – 4810Combined sources
Beta strandi51 – 588Combined sources
Helixi60 – 634Combined sources
Beta strandi80 – 867Combined sources
Beta strandi91 – 999Combined sources
Beta strandi104 – 11613Combined sources
Helixi177 – 19317Combined sources
Helixi199 – 2057Combined sources
Helixi210 – 22011Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1BBYNMR-A175-243[»]
1F3UX-ray1.70A/C/E/G2-119[»]
2BBYNMR-A175-243[»]
5IY6electron microscopy7.20T1-249[»]
5IY7electron microscopy8.60T1-249[»]
5IY8electron microscopy7.90T1-249[»]
5IY9electron microscopy6.30T1-249[»]
5IYAelectron microscopy5.40T1-249[»]
5IYBelectron microscopy3.90T1-249[»]
5IYCelectron microscopy3.90T1-249[»]
5IYDelectron microscopy3.90T1-249[»]
ProteinModelPortaliP13984.
SMRiP13984. Positions 2-119, 175-243.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP13984.

Family & Domainsi

Sequence similaritiesi

Belongs to the TFIIF beta subunit family.Curated

Phylogenomic databases

eggNOGiKOG2905. Eukaryota.
COG5090. LUCA.
GeneTreeiENSGT00390000016051.
HOGENOMiHOG000294179.
HOVERGENiHBG001606.
InParanoidiP13984.
KOiK03139.
OMAiIANKWEK.
OrthoDBiEOG091G0IN2.
PhylomeDBiP13984.
TreeFamiTF314290.

Family and domain databases

Gene3Di1.10.10.10. 1 hit.
InterProiIPR003196. TFIIF_beta.
IPR011039. TFIIF_interaction.
IPR011991. WHTH_DNA-bd_dom.
[Graphical view]
PANTHERiPTHR10445. PTHR10445. 1 hit.
PfamiPF02270. TFIIF_beta. 1 hit.
[Graphical view]
PIRSFiPIRSF015849. TFIIF-beta. 1 hit.
SUPFAMiSSF46785. 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]FASTAAdd 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.
CCDSiCCDS9395.1.
PIRiS06141.
S18677.
RefSeqiNP_004119.1. NM_004128.2.
UniGeneiHs.654582.

Genome annotation databases

EnsembliENST00000340473; ENSP00000340823; ENSG00000188342.
GeneIDi2963.
KEGGihsa:2963.
UCSCiuc001uzw.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.
CCDSiCCDS9395.1.
PIRiS06141.
S18677.
RefSeqiNP_004119.1. NM_004128.2.
UniGeneiHs.654582.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1BBYNMR-A175-243[»]
1F3UX-ray1.70A/C/E/G2-119[»]
2BBYNMR-A175-243[»]
5IY6electron microscopy7.20T1-249[»]
5IY7electron microscopy8.60T1-249[»]
5IY8electron microscopy7.90T1-249[»]
5IY9electron microscopy6.30T1-249[»]
5IYAelectron microscopy5.40T1-249[»]
5IYBelectron microscopy3.90T1-249[»]
5IYCelectron microscopy3.90T1-249[»]
5IYDelectron microscopy3.90T1-249[»]
ProteinModelPortaliP13984.
SMRiP13984. Positions 2-119, 175-243.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi109218. 51 interactions.
DIPiDIP-41680N.
IntActiP13984. 38 interactions.
MINTiMINT-193667.
STRINGi9606.ENSP00000340823.

PTM databases

iPTMnetiP13984.
PhosphoSiteiP13984.

Polymorphism and mutation databases

BioMutaiGTF2F2.
DMDMi464519.

Proteomic databases

EPDiP13984.
MaxQBiP13984.
PaxDbiP13984.
PeptideAtlasiP13984.
PRIDEiP13984.

Protocols and materials databases

DNASUi2963.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000340473; ENSP00000340823; ENSG00000188342.
GeneIDi2963.
KEGGihsa:2963.
UCSCiuc001uzw.4. human.

Organism-specific databases

CTDi2963.
GeneCardsiGTF2F2.
HGNCiHGNC:4653. GTF2F2.
HPAiHPA006912.
MIMi189969. gene.
neXtProtiNX_P13984.
PharmGKBiPA29039.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiKOG2905. Eukaryota.
COG5090. LUCA.
GeneTreeiENSGT00390000016051.
HOGENOMiHOG000294179.
HOVERGENiHBG001606.
InParanoidiP13984.
KOiK03139.
OMAiIANKWEK.
OrthoDBiEOG091G0IN2.
PhylomeDBiP13984.
TreeFamiTF314290.

Enzyme and pathway databases

ReactomeiR-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

ChiTaRSiGTF2F2. human.
EvolutionaryTraceiP13984.
GeneWikiiGTF2F2.
GenomeRNAii2963.
PROiP13984.
SOURCEiSearch...

Gene expression databases

BgeeiENSG00000188342.
CleanExiHS_GTF2F2.
ExpressionAtlasiP13984. baseline and differential.
GenevisibleiP13984. HS.

Family and domain databases

Gene3Di1.10.10.10. 1 hit.
InterProiIPR003196. TFIIF_beta.
IPR011039. TFIIF_interaction.
IPR011991. WHTH_DNA-bd_dom.
[Graphical view]
PANTHERiPTHR10445. PTHR10445. 1 hit.
PfamiPF02270. TFIIF_beta. 1 hit.
[Graphical view]
PIRSFiPIRSF015849. TFIIF-beta. 1 hit.
SUPFAMiSSF46785. SSF46785. 1 hit.
SSF50916. SSF50916. 1 hit.
ProtoNetiSearch...

Entry informationi

Entry nameiT2FB_HUMAN
AccessioniPrimary (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 statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny 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

  1. Human chromosome 13
    Human chromosome 13: entries, gene names and cross-references to MIM
  2. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  3. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  4. 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.