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Protein

General transcription factor IIF subunit 1

Gene

GTF2F1

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.1 Publication

GO - Molecular functioni

  • catalytic activity Source: InterPro
  • DNA binding Source: UniProtKB-KW
  • phosphatase activator activity Source: UniProtKB
  • poly(A) RNA binding Source: UniProtKB
  • transcription coactivator activity Source: ProtInc
  • transcription factor binding Source: BHF-UCL

GO - Biological processi

Complete GO annotation...

Keywords - Biological processi

Transcription, Transcription regulation

Keywords - Ligandi

DNA-binding

Enzyme and pathway databases

BioCyciZFISH:ENSG00000125651-MONOMER.
ReactomeiR-HSA-112382. Formation of RNA Pol II elongation complex.
R-HSA-112387. Elongation arrest and recovery.
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.
SIGNORiP35269.

Names & Taxonomyi

Protein namesi
Recommended name:
General transcription factor IIF subunit 1
Alternative name(s):
General transcription factor IIF 74 kDa subunit
Transcription initiation factor IIF subunit alpha
Short name:
TFIIF-alpha
Transcription initiation factor RAP74
Gene namesi
Name:GTF2F1
Synonyms:RAP74
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
Proteomesi
  • UP000005640 Componenti: Chromosome 19

Organism-specific databases

HGNCiHGNC:4652. GTF2F1.

Subcellular locationi

GO - Cellular componenti

  • cell junction Source: HPA
  • intracellular membrane-bounded organelle Source: HPA
  • nucleoplasm Source: Reactome
  • nucleus Source: HPA
  • transcription factor TFIID complex Source: UniProtKB
  • transcription factor TFIIF complex Source: ProtInc
Complete GO annotation...

Keywords - Cellular componenti

Nucleus

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Mutagenesisi385S → A: Eliminates putative kinase activity; when associated with A-389. 1 Publication1
Mutagenesisi389T → A: Eliminates putative kinase activity; when associated with A-385. 1 Publication1

Organism-specific databases

DisGeNETi2962.
OpenTargetsiENSG00000125651.
PharmGKBiPA29038.

Polymorphism and mutation databases

BioMutaiGTF2F1.
DMDMi46397744.

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Initiator methionineiRemovedCombined sources
ChainiPRO_00002112312 – 517General transcription factor IIF subunit 1Add BLAST516

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei2N-acetylalanineCombined sources1
Modified residuei156PhosphothreonineCombined sources1
Modified residuei217PhosphoserineCombined sources1
Modified residuei218PhosphoserineCombined sources1
Modified residuei221PhosphoserineCombined sources1
Modified residuei224PhosphoserineCombined sources1
Modified residuei331PhosphothreonineCombined sources1
Modified residuei377PhosphoserineCombined sources1
Modified residuei380PhosphoserineCombined sources1
Modified residuei381PhosphoserineCombined sources1
Modified residuei385PhosphoserineCombined sources1 Publication1
Modified residuei389PhosphothreonineCombined sources1 Publication1
Modified residuei391PhosphoserineCombined sources1
Modified residuei407N6-acetyllysineCombined sources1
Modified residuei431PhosphoserineCombined sources1
Modified residuei433PhosphoserineCombined sources1
Modified residuei436PhosphoserineCombined sources1
Modified residuei437PhosphothreonineCombined sources1
Modified residuei446PhosphothreonineCombined sources1
Modified residuei449PhosphoserineCombined sources1

Post-translational modificationi

Phosphorylated on Ser and other residues by TAF1 and casein kinase II-like kinases.2 Publications

Keywords - PTMi

Acetylation, Phosphoprotein

Proteomic databases

EPDiP35269.
MaxQBiP35269.
PaxDbiP35269.
PeptideAtlasiP35269.
PRIDEiP35269.
TopDownProteomicsiP35269.

PTM databases

iPTMnetiP35269.
PhosphoSitePlusiP35269.

Miscellaneous databases

PMAP-CutDBP35269.

Expressioni

Inductioni

Up-regulated in response to enterovirus 71 (EV71) infection.1 Publication

Gene expression databases

BgeeiENSG00000125651.
CleanExiHS_GTF2F1.
ExpressionAtlasiP35269. baseline and differential.
GenevisibleiP35269. HS.

Organism-specific databases

HPAiHPA022793.
HPA028707.

Interactioni

Subunit structurei

Heterodimer of an alpha and a beta subunit. Interacts with GTF2F2, CTDP1, TAF6/TAFII80 and URI1.4 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
TAF1P216753EBI-457886,EBI-491289
URI1O947633EBI-457886,EBI-357067

GO - Molecular functioni

  • transcription factor binding Source: BHF-UCL

Protein-protein interaction databases

BioGridi109217. 98 interactors.
DIPiDIP-677N.
IntActiP35269. 21 interactors.
MINTiMINT-1403790.
STRINGi9606.ENSP00000377969.

Structurei

Secondary structure

1517
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Beta strandi10 – 17Combined sources8
Beta strandi23 – 31Combined sources9
Helixi33 – 35Combined sources3
Helixi39 – 41Combined sources3
Beta strandi45 – 49Combined sources5
Helixi52 – 55Combined sources4
Beta strandi58 – 61Combined sources4
Helixi76 – 78Combined sources3
Beta strandi84 – 87Combined sources4
Beta strandi98 – 104Combined sources7
Beta strandi109 – 114Combined sources6
Beta strandi120 – 129Combined sources10
Beta strandi135 – 148Combined sources14
Helixi149 – 151Combined sources3
Helixi157 – 167Combined sources11
Helixi456 – 465Combined sources10
Helixi470 – 475Combined sources6
Helixi479 – 482Combined sources4
Helixi486 – 500Combined sources15
Beta strandi503 – 507Combined sources5
Beta strandi510 – 515Combined sources6

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1F3UX-ray1.70B/D/F/H2-172[»]
1I27X-ray1.02A449-517[»]
1J2XX-ray2.00A449-517[»]
1NHANMR-A436-517[»]
1ONVNMR-A436-517[»]
2K7LNMR-A451-517[»]
5IY6electron microscopy7.20S1-517[»]
5IY7electron microscopy8.60S1-517[»]
5IY8electron microscopy7.90S1-517[»]
5IY9electron microscopy6.30S1-517[»]
5IYAelectron microscopy5.40S1-517[»]
5IYBelectron microscopy3.90S1-517[»]
5IYCelectron microscopy3.90S1-517[»]
5IYDelectron microscopy3.90S1-517[»]
ProteinModelPortaliP35269.
SMRiP35269.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP35269.

Family & Domainsi

Compositional bias

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Compositional biasi283 – 350Glu-richAdd BLAST68

Sequence similaritiesi

Belongs to the TFIIF alpha subunit family.Curated

Phylogenomic databases

eggNOGiKOG2393. Eukaryota.
ENOG410XSRW. LUCA.
GeneTreeiENSGT00440000038032.
HOGENOMiHOG000059644.
HOVERGENiHBG000729.
InParanoidiP35269.
KOiK03138.
OMAiPERKMIS.
OrthoDBiEOG091G0N3J.
PhylomeDBiP35269.
TreeFamiTF313850.

Family and domain databases

Gene3Di1.10.10.10. 1 hit.
InterProiIPR008851. TFIIF-alpha.
IPR011039. TFIIF_interaction.
IPR011991. WHTH_DNA-bd_dom.
[Graphical view]
PfamiPF05793. TFIIF_alpha. 1 hit.
[Graphical view]
SUPFAMiSSF46785. SSF46785. 1 hit.
SSF50916. SSF50916. 2 hits.

Sequencei

Sequence statusi: Complete.

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

P35269-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MAALGPSSQN VTEYVVRVPK NTTKKYNIMA FNAADKVNFA TWNQARLERD
60 70 80 90 100
LSNKKIYQEE EMPESGAGSE FNRKLREEAR RKKYGIVLKE FRPEDQPWLL
110 120 130 140 150
RVNGKSGRKF KGIKKGGVTE NTSYYIFTQC PDGAFEAFPV HNWYNFTPLA
160 170 180 190 200
RHRTLTAEEA EEEWERRNKV LNHFSIMQQR RLKDQDQDED EEEKEKRGRR
210 220 230 240 250
KASELRIHDL EDDLEMSSDA SDASGEEGGR VPKAKKKAPL AKGGRKKKKK
260 270 280 290 300
KGSDDEAFED SDDGDFEGQE VDYMSDGSSS SQEEPESKAK APQQEEGPKG
310 320 330 340 350
VDEQSDSSEE SEEEKPPEED KEEEEEKKAP TPQEKKRRKD SSEESDSSEE
360 370 380 390 400
SDIDSEASSA LFMAKKKTPP KRERKPSGGS SRGNSRPGTP SAEGGSTSST
410 420 430 440 450
LRAAASKLEQ GKRVSEMPAA KRLRLDTGPQ SLSGKSTPQP PSGKTTPNSG
460 470 480 490 500
DVQVTEDAVR RYLTRKPMTT KDLLKKFQTK KTGLSSEQTV NVLAQILKRL
510
NPERKMINDK MHFSLKE
Length:517
Mass (Da):58,240
Last modified:April 13, 2004 - v2
Checksum:i1032B04A36BDC24F
GO

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sequence conflicti231V → I in CAA45404 (PubMed:1734284).Curated1
Sequence conflicti361L → F in CAA45408 (PubMed:1734283).Curated1

Natural variant

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Natural variantiVAR_0390043A → V.Corresponds to variant rs34826931dbSNPEnsembl.1

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X64037 mRNA. Translation: CAA45408.1.
X64002 mRNA. Translation: CAA45404.1.
BT007097 mRNA. Translation: AAP35761.1.
AK315240 mRNA. Translation: BAG37667.1.
CH471139 Genomic DNA. Translation: EAW69098.1.
BC000120 mRNA. Translation: AAH00120.1.
BC013007 mRNA. Translation: AAH13007.1.
CCDSiCCDS12165.1.
PIRiS20248.
RefSeqiNP_002087.2. NM_002096.2.
UniGeneiHs.68257.

Genome annotation databases

EnsembliENST00000394456; ENSP00000377969; ENSG00000125651.
GeneIDi2962.
KEGGihsa:2962.
UCSCiuc002meq.3. human.

Keywords - Coding sequence diversityi

Polymorphism

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X64037 mRNA. Translation: CAA45408.1.
X64002 mRNA. Translation: CAA45404.1.
BT007097 mRNA. Translation: AAP35761.1.
AK315240 mRNA. Translation: BAG37667.1.
CH471139 Genomic DNA. Translation: EAW69098.1.
BC000120 mRNA. Translation: AAH00120.1.
BC013007 mRNA. Translation: AAH13007.1.
CCDSiCCDS12165.1.
PIRiS20248.
RefSeqiNP_002087.2. NM_002096.2.
UniGeneiHs.68257.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1F3UX-ray1.70B/D/F/H2-172[»]
1I27X-ray1.02A449-517[»]
1J2XX-ray2.00A449-517[»]
1NHANMR-A436-517[»]
1ONVNMR-A436-517[»]
2K7LNMR-A451-517[»]
5IY6electron microscopy7.20S1-517[»]
5IY7electron microscopy8.60S1-517[»]
5IY8electron microscopy7.90S1-517[»]
5IY9electron microscopy6.30S1-517[»]
5IYAelectron microscopy5.40S1-517[»]
5IYBelectron microscopy3.90S1-517[»]
5IYCelectron microscopy3.90S1-517[»]
5IYDelectron microscopy3.90S1-517[»]
ProteinModelPortaliP35269.
SMRiP35269.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi109217. 98 interactors.
DIPiDIP-677N.
IntActiP35269. 21 interactors.
MINTiMINT-1403790.
STRINGi9606.ENSP00000377969.

PTM databases

iPTMnetiP35269.
PhosphoSitePlusiP35269.

Polymorphism and mutation databases

BioMutaiGTF2F1.
DMDMi46397744.

Proteomic databases

EPDiP35269.
MaxQBiP35269.
PaxDbiP35269.
PeptideAtlasiP35269.
PRIDEiP35269.
TopDownProteomicsiP35269.

Protocols and materials databases

DNASUi2962.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000394456; ENSP00000377969; ENSG00000125651.
GeneIDi2962.
KEGGihsa:2962.
UCSCiuc002meq.3. human.

Organism-specific databases

CTDi2962.
DisGeNETi2962.
GeneCardsiGTF2F1.
HGNCiHGNC:4652. GTF2F1.
HPAiHPA022793.
HPA028707.
MIMi189968. gene.
neXtProtiNX_P35269.
OpenTargetsiENSG00000125651.
PharmGKBiPA29038.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiKOG2393. Eukaryota.
ENOG410XSRW. LUCA.
GeneTreeiENSGT00440000038032.
HOGENOMiHOG000059644.
HOVERGENiHBG000729.
InParanoidiP35269.
KOiK03138.
OMAiPERKMIS.
OrthoDBiEOG091G0N3J.
PhylomeDBiP35269.
TreeFamiTF313850.

Enzyme and pathway databases

BioCyciZFISH:ENSG00000125651-MONOMER.
ReactomeiR-HSA-112382. Formation of RNA Pol II elongation complex.
R-HSA-112387. Elongation arrest and recovery.
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.
SIGNORiP35269.

Miscellaneous databases

ChiTaRSiGTF2F1. human.
EvolutionaryTraceiP35269.
GeneWikiiGTF2F1.
GenomeRNAii2962.
PMAP-CutDBP35269.
PROiP35269.
SOURCEiSearch...

Gene expression databases

BgeeiENSG00000125651.
CleanExiHS_GTF2F1.
ExpressionAtlasiP35269. baseline and differential.
GenevisibleiP35269. HS.

Family and domain databases

Gene3Di1.10.10.10. 1 hit.
InterProiIPR008851. TFIIF-alpha.
IPR011039. TFIIF_interaction.
IPR011991. WHTH_DNA-bd_dom.
[Graphical view]
PfamiPF05793. TFIIF_alpha. 1 hit.
[Graphical view]
SUPFAMiSSF46785. SSF46785. 1 hit.
SSF50916. SSF50916. 2 hits.
ProtoNetiSearch...

Entry informationi

Entry nameiT2FA_HUMAN
AccessioniPrimary (citable) accession number: P35269
Secondary accession number(s): B2RCS0, Q9BWN0
Entry historyi
Integrated into UniProtKB/Swiss-Prot: February 1, 1994
Last sequence update: April 13, 2004
Last modified: November 30, 2016
This is version 176 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

Caution

Was reported to have a protein kinase activity and to autophosphorylates on Ser-385 and Thr-389.1 Publication

Keywords - Technical termi

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

Documents

  1. Human chromosome 19
    Human chromosome 19: entries, gene names and cross-references to MIM
  2. Human entries with polymorphisms or disease mutations
    List of human entries with polymorphisms or disease mutations
  3. Human polymorphisms and disease mutations
    Index of human polymorphisms and disease mutations
  4. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  5. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  6. 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.