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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

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.
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

Complete GO annotation...

Keywords - Cellular componenti

Nucleus

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi385 – 3851S → A: Eliminates putative kinase activity; when associated with A-389. 1 Publication
Mutagenesisi389 – 3891T → A: Eliminates putative kinase activity; when associated with A-385. 1 Publication

Organism-specific databases

PharmGKBiPA29038.

Polymorphism and mutation databases

BioMutaiGTF2F1.
DMDMi46397744.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methionineiRemovedCombined sources
Chaini2 – 517516General transcription factor IIF subunit 1PRO_0000211231Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei2 – 21N-acetylalanineCombined sources
Modified residuei156 – 1561PhosphothreonineCombined sources
Modified residuei217 – 2171PhosphoserineCombined sources
Modified residuei218 – 2181PhosphoserineCombined sources
Modified residuei221 – 2211PhosphoserineCombined sources
Modified residuei224 – 2241PhosphoserineCombined sources
Modified residuei331 – 3311PhosphothreonineCombined sources
Modified residuei377 – 3771PhosphoserineCombined sources
Modified residuei380 – 3801PhosphoserineCombined sources
Modified residuei381 – 3811PhosphoserineCombined sources
Modified residuei385 – 3851PhosphoserineCombined sources1 Publication
Modified residuei389 – 3891PhosphothreonineCombined sources1 Publication
Modified residuei391 – 3911PhosphoserineCombined sources
Modified residuei407 – 4071N6-acetyllysineCombined sources
Modified residuei431 – 4311PhosphoserineCombined sources
Modified residuei433 – 4331PhosphoserineCombined sources
Modified residuei436 – 4361PhosphoserineCombined sources
Modified residuei437 – 4371PhosphothreonineCombined sources
Modified residuei446 – 4461PhosphothreonineCombined sources
Modified residuei449 – 4491PhosphoserineCombined sources

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.
PhosphoSiteiP35269.

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 interactions.
DIPiDIP-677N.
IntActiP35269. 21 interactions.
MINTiMINT-1403790.
STRINGi9606.ENSP00000377969.

Structurei

Secondary structure

1
517
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi10 – 178Combined sources
Beta strandi23 – 319Combined sources
Helixi33 – 353Combined sources
Helixi39 – 413Combined sources
Beta strandi45 – 495Combined sources
Helixi52 – 554Combined sources
Beta strandi58 – 614Combined sources
Helixi76 – 783Combined sources
Beta strandi84 – 874Combined sources
Beta strandi98 – 1047Combined sources
Beta strandi109 – 1146Combined sources
Beta strandi120 – 12910Combined sources
Beta strandi135 – 14814Combined sources
Helixi149 – 1513Combined sources
Helixi157 – 16711Combined sources
Helixi456 – 46510Combined sources
Helixi470 – 4756Combined sources
Helixi479 – 4824Combined sources
Helixi486 – 50015Combined sources
Beta strandi503 – 5075Combined sources
Beta strandi510 – 5156Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
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. Positions 7-168, 449-517.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP35269.

Family & Domainsi

Compositional bias

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Compositional biasi283 – 35068Glu-richAdd
BLAST

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)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti231 – 2311V → I in CAA45404 (PubMed:1734284).Curated
Sequence conflicti361 – 3611L → F in CAA45408 (PubMed:1734283).Curated

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti3 – 31A → V.
Corresponds to variant rs34826931 [ dbSNP | Ensembl ].
VAR_039004

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
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. Positions 7-168, 449-517.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

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

PTM databases

iPTMnetiP35269.
PhosphoSiteiP35269.

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

Phylogenomic databases

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

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.
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: September 7, 2016
This is version 173 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.