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Protein

Transcription initiation factor IIA subunit 1

Gene

GTF2A1

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

Functioni

TFIIA is a component of the transcription machinery of RNA polymerase II and plays an important role in transcriptional activation. TFIIA in a complex with TBP mediates transcriptional activity.2 Publications

GO - Molecular functioni

  • DNA binding Source: BHF-UCL
  • protein heterodimerization activity Source: BHF-UCL
  • TBP-class protein binding Source: BHF-UCL
  • transcription coactivator activity Source: ProtInc
  • transcription factor binding Source: BHF-UCL

GO - Biological processi

Complete GO annotation...

Keywords - Biological processi

Transcription, Transcription regulation

Enzyme and pathway databases

BioCyciZFISH:ENSG00000165417-MONOMER.
ReactomeiR-HSA-167161. HIV Transcription Initiation.
R-HSA-167162. RNA Polymerase II HIV Promoter Escape.
R-HSA-167172. Transcription of the HIV genome.
R-HSA-674695. RNA Polymerase II Pre-transcription Events.
R-HSA-6807505. RNA polymerase II transcribes snRNA genes.
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-76042. RNA Polymerase II Transcription Initiation And Promoter Clearance.
SIGNORiP52655.

Names & Taxonomyi

Protein namesi
Recommended name:
Transcription initiation factor IIA subunit 1
Alternative name(s):
General transcription factor IIA subunit 1
TFIIAL
Transcription initiation factor TFIIA 42 kDa subunit
Short name:
TFIIA-42
Cleaved into the following 2 chains:
Alternative name(s):
TFIIA p35 subunit
Alternative name(s):
TFIIA p19 subunit
Gene namesi
Name:GTF2A1
Synonyms:TF2A1
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
Proteomesi
  • UP000005640 Componenti: Chromosome 14

Organism-specific databases

HGNCiHGNC:4646. GTF2A1.

Subcellular locationi

GO - Cellular componenti

  • cytoplasm Source: HPA
  • nucleoplasm Source: HPA
  • transcription factor TFIIA complex Source: BHF-UCL
  • transcription factor TFIID complex Source: UniProtKB
Complete GO annotation...

Keywords - Cellular componenti

Nucleus

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Mutagenesisi270V → A: Slightly affects cleavage and yields elevated levels of the precursor. 1 Publication1
Mutagenesisi272Q → A: Abolishes cleavage. 1 Publication1
Mutagenesisi273V → A: Abolishes cleavage. 1 Publication1
Mutagenesisi274D → A: Abolishes cleavage. 1 Publication1
Mutagenesisi275G → A: Abolishes cleavage. 1 Publication1
Mutagenesisi276T → A: Does not affect cleavage. 1 Publication1
Mutagenesisi277G → A: Does not affect cleavage. 1 Publication1
Mutagenesisi278D → A: Significant reduction of cleavage. 1 Publication1
Mutagenesisi280S → A: Slightly affects cleavage, yields elevated levels of the precursor. Eliminates phosphorylation; when associated with A-281; A-316 and A-321. 2 Publications1
Mutagenesisi281S → A: Eliminates phosphorylation; when associated with A-280; A-316 and A-321. 1 Publication1
Mutagenesisi282E → A: Slightly affects cleavage and yields elevated levels of the precursor. 1 Publication1
Mutagenesisi316S → A: Strongly reduces phosphorylation; when associated with A-321. Eliminates phosphorylation; when associated with A-280; A-281 and A-321. 1 Publication1
Mutagenesisi321S → A: Strongly reduces phosphorylation; when associated with A-316. Eliminates phosphorylation; when associated with A-280; A-281 and A-316. 1 Publication1

Organism-specific databases

DisGeNETi2957.
OpenTargetsiENSG00000165417.
PharmGKBiPA29033.

Chemistry databases

ChEMBLiCHEMBL4832.

Polymorphism and mutation databases

BioMutaiGTF2A1.
DMDMi1711663.

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Initiator methionineiRemovedCombined sources
ChainiPRO_00000224812 – 376Transcription initiation factor IIA subunit 1Add BLAST375
ChainiPRO_00000425932 – 274Transcription initiation factor IIA alpha chainAdd BLAST273
ChainiPRO_0000042594275 – 376Transcription initiation factor IIA beta chainAdd BLAST102

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei2N-acetylalanineCombined sources1
Modified residuei280Phosphoserine; by TAF11 Publication1
Modified residuei281Phosphoserine; by TAF11 Publication1
Modified residuei316Phosphoserine; by TAF1Combined sources1 Publication1
Modified residuei321Phosphoserine; by TAF1Combined sources1 Publication1

Post-translational modificationi

The alpha and beta subunits are postranslationally produced from the precursor form by TASP1. The cleavage promotes proteasomal degradation.1 Publication

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sitei274 – 275Cleavage; by TASP12

Keywords - PTMi

Acetylation, Phosphoprotein

Proteomic databases

EPDiP52655.
MaxQBiP52655.
PaxDbiP52655.
PeptideAtlasiP52655.
PRIDEiP52655.

PTM databases

iPTMnetiP52655.
PhosphoSitePlusiP52655.

Miscellaneous databases

PMAP-CutDBP52655.

Expressioni

Gene expression databases

BgeeiENSG00000165417.
ExpressionAtlasiP52655. baseline and differential.
GenevisibleiP52655. HS.

Organism-specific databases

HPAiHPA000869.

Interactioni

Subunit structurei

TFIIA is a heterodimer of the large unprocessed subunit 1 and a small subunit gamma. It was originally believed to be a heterotrimer of an alpha (p35), a beta (p19) and a gamma subunit (p12). TFIIA forms a complex with TBP.1 Publication

Binary interactionsi

WithEntry#Exp.IntActNotes
GTF2A2P526576EBI-389518,EBI-1045262
NFYAP235113EBI-389518,EBI-389739

GO - Molecular functioni

  • protein heterodimerization activity Source: BHF-UCL
  • TBP-class protein binding Source: BHF-UCL
  • transcription factor binding Source: BHF-UCL

Protein-protein interaction databases

BioGridi109212. 54 interactors.
DIPiDIP-33225N.
IntActiP52655. 11 interactors.
STRINGi9606.ENSP00000452454.

Chemistry databases

BindingDBiP52655.

Structurei

Secondary structure

1376
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Helixi10 – 32Combined sources23
Helixi36 – 50Combined sources15
Beta strandi334 – 345Combined sources12
Beta strandi348 – 360Combined sources13
Beta strandi363 – 375Combined sources13

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1NVPX-ray2.10B2-58[»]
C303-376[»]
5FURelectron microscopy8.50B9-51[»]
C330-376[»]
5IY6electron microscopy7.20N1-376[»]
5IY7electron microscopy8.60N1-376[»]
5IY8electron microscopy7.90N1-376[»]
5IY9electron microscopy6.30N1-376[»]
5IYAelectron microscopy5.40N1-376[»]
5IYBelectron microscopy3.90N1-376[»]
5IYCelectron microscopy3.90N1-376[»]
5IYDelectron microscopy3.90N1-376[»]
ProteinModelPortaliP52655.
SMRiP52655.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP52655.

Family & Domainsi

Compositional bias

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Compositional biasi71 – 80Poly-Gln10
Compositional biasi81 – 87Poly-His7

Sequence similaritiesi

Belongs to the TFIIA subunit 1 family.Curated

Phylogenomic databases

eggNOGiENOG410IPCF. Eukaryota.
ENOG4111M8K. LUCA.
GeneTreeiENSGT00830000128302.
HOGENOMiHOG000015236.
HOVERGENiHBG052771.
InParanoidiP52655.
KOiK03122.
OMAiKAPRFAS.
OrthoDBiEOG091G0GC2.
PhylomeDBiP52655.
TreeFamiTF350445.

Family and domain databases

CDDicd07976. TFIIA_alpha_beta_like. 2 hits.
Gene3Di1.10.287.100. 1 hit.
2.30.18.10. 1 hit.
InterProiIPR009083. TFIIA_a-hlx.
IPR004855. TFIIA_asu/bsu.
IPR013028. TFIIA_asu_N.
IPR009088. TFIIA_b-brl.
[Graphical view]
PANTHERiPTHR12694. PTHR12694. 1 hit.
PfamiPF03153. TFIIA. 2 hits.
[Graphical view]
SMARTiSM01371. TFIIA. 1 hit.
[Graphical view]
SUPFAMiSSF47396. SSF47396. 1 hit.
SSF50784. SSF50784. 1 hit.

Sequences (2)i

Sequence statusi: Complete.

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

This entry describes 2 isoformsi produced by alternative initiation. AlignAdd to basket

Isoform 42 kDa (identifier: P52655-1) [UniParc]FASTAAdd to basket

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

« Hide

        10         20         30         40         50
MANSANTNTV PKLYRSVIED VINDVRDIFL DDGVDEQVLM ELKTLWENKL
60 70 80 90 100
MQSRAVDGFH SEEQQLLLQV QQQHQPQQQQ HHHHHHHQQA QPQQTVPQQA
110 120 130 140 150
QTQQVLIPAS QQATAPQVIV PDSKLIQHMN ASNMSAAATA ATLALPAGVT
160 170 180 190 200
PVQQILTNSG QLLQVVRAAN GAQYIFQPQQ SVVLQQQVIP QMQPGGVQAP
210 220 230 240 250
VIQQVLAPLP GGISPQTGVI IQPQQILFTG NKTQVIPTTV AAPTPAQAQI
260 270 280 290 300
TATGQQQPQA QPAQTQAPLV LQVDGTGDTS SEEDEDEEED YDDDEEEDKE
310 320 330 340 350
KDGAEDGQVE EEPLNSEDDV SDEEGQELFD TENVVVCQYD KIHRSKNKWK
360 370
FHLKDGIMNL NGRDYIFSKA IGDAEW
Length:376
Mass (Da):41,514
Last modified:October 1, 1996 - v1
Checksum:i4BAE1853E7E89218
GO
Isoform 37 kDa (identifier: P52655-2) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     1-39: Missing.

Show »
Length:337
Mass (Da):37,152
Checksum:i81D62BCC81399DE6
GO

Natural variant

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Natural variantiVAR_03566730L → V in a breast cancer sample; somatic mutation. 1 Publication1
Natural variantiVAR_054043109A → P.Corresponds to variant rs17111579dbSNPEnsembl.1

Alternative sequence

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Alternative sequenceiVSP_0187981 – 39Missing in isoform 37 kDa. CuratedAdd BLAST39

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X75383 mRNA. Translation: CAA53151.1.
X75383 mRNA. Translation: CAA53152.1.
X77225 mRNA. Translation: CAA54442.1.
D14887 mRNA. Translation: BAA03604.1.
D14886 mRNA. Translation: BAA03603.1.
AC010582 Genomic DNA. Translation: AAF26776.1.
BC107155 mRNA. Translation: AAI07156.1.
BC107156 mRNA. Translation: AAI07157.1.
CCDSiCCDS9873.1. [P52655-1]
CCDS9874.1. [P52655-2]
PIRiA49077.
RefSeqiNP_001265869.1. NM_001278940.1.
NP_056943.1. NM_015859.3. [P52655-1]
NP_963889.1. NM_201595.2. [P52655-2]
UniGeneiHs.592334.

Genome annotation databases

EnsembliENST00000434192; ENSP00000409492; ENSG00000165417. [P52655-2]
ENST00000553612; ENSP00000452454; ENSG00000165417. [P52655-1]
GeneIDi2957.
KEGGihsa:2957.
UCSCiuc001xvf.4. human. [P52655-1]

Keywords - Coding sequence diversityi

Alternative initiation, Polymorphism

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X75383 mRNA. Translation: CAA53151.1.
X75383 mRNA. Translation: CAA53152.1.
X77225 mRNA. Translation: CAA54442.1.
D14887 mRNA. Translation: BAA03604.1.
D14886 mRNA. Translation: BAA03603.1.
AC010582 Genomic DNA. Translation: AAF26776.1.
BC107155 mRNA. Translation: AAI07156.1.
BC107156 mRNA. Translation: AAI07157.1.
CCDSiCCDS9873.1. [P52655-1]
CCDS9874.1. [P52655-2]
PIRiA49077.
RefSeqiNP_001265869.1. NM_001278940.1.
NP_056943.1. NM_015859.3. [P52655-1]
NP_963889.1. NM_201595.2. [P52655-2]
UniGeneiHs.592334.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1NVPX-ray2.10B2-58[»]
C303-376[»]
5FURelectron microscopy8.50B9-51[»]
C330-376[»]
5IY6electron microscopy7.20N1-376[»]
5IY7electron microscopy8.60N1-376[»]
5IY8electron microscopy7.90N1-376[»]
5IY9electron microscopy6.30N1-376[»]
5IYAelectron microscopy5.40N1-376[»]
5IYBelectron microscopy3.90N1-376[»]
5IYCelectron microscopy3.90N1-376[»]
5IYDelectron microscopy3.90N1-376[»]
ProteinModelPortaliP52655.
SMRiP52655.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi109212. 54 interactors.
DIPiDIP-33225N.
IntActiP52655. 11 interactors.
STRINGi9606.ENSP00000452454.

Chemistry databases

BindingDBiP52655.
ChEMBLiCHEMBL4832.

PTM databases

iPTMnetiP52655.
PhosphoSitePlusiP52655.

Polymorphism and mutation databases

BioMutaiGTF2A1.
DMDMi1711663.

Proteomic databases

EPDiP52655.
MaxQBiP52655.
PaxDbiP52655.
PeptideAtlasiP52655.
PRIDEiP52655.

Protocols and materials databases

DNASUi2957.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000434192; ENSP00000409492; ENSG00000165417. [P52655-2]
ENST00000553612; ENSP00000452454; ENSG00000165417. [P52655-1]
GeneIDi2957.
KEGGihsa:2957.
UCSCiuc001xvf.4. human. [P52655-1]

Organism-specific databases

CTDi2957.
DisGeNETi2957.
GeneCardsiGTF2A1.
HGNCiHGNC:4646. GTF2A1.
HPAiHPA000869.
MIMi600520. gene.
neXtProtiNX_P52655.
OpenTargetsiENSG00000165417.
PharmGKBiPA29033.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiENOG410IPCF. Eukaryota.
ENOG4111M8K. LUCA.
GeneTreeiENSGT00830000128302.
HOGENOMiHOG000015236.
HOVERGENiHBG052771.
InParanoidiP52655.
KOiK03122.
OMAiKAPRFAS.
OrthoDBiEOG091G0GC2.
PhylomeDBiP52655.
TreeFamiTF350445.

Enzyme and pathway databases

BioCyciZFISH:ENSG00000165417-MONOMER.
ReactomeiR-HSA-167161. HIV Transcription Initiation.
R-HSA-167162. RNA Polymerase II HIV Promoter Escape.
R-HSA-167172. Transcription of the HIV genome.
R-HSA-674695. RNA Polymerase II Pre-transcription Events.
R-HSA-6807505. RNA polymerase II transcribes snRNA genes.
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-76042. RNA Polymerase II Transcription Initiation And Promoter Clearance.
SIGNORiP52655.

Miscellaneous databases

ChiTaRSiGTF2A1. human.
EvolutionaryTraceiP52655.
GeneWikiiGTF2A1.
GenomeRNAii2957.
PMAP-CutDBP52655.
PROiP52655.
SOURCEiSearch...

Gene expression databases

BgeeiENSG00000165417.
ExpressionAtlasiP52655. baseline and differential.
GenevisibleiP52655. HS.

Family and domain databases

CDDicd07976. TFIIA_alpha_beta_like. 2 hits.
Gene3Di1.10.287.100. 1 hit.
2.30.18.10. 1 hit.
InterProiIPR009083. TFIIA_a-hlx.
IPR004855. TFIIA_asu/bsu.
IPR013028. TFIIA_asu_N.
IPR009088. TFIIA_b-brl.
[Graphical view]
PANTHERiPTHR12694. PTHR12694. 1 hit.
PfamiPF03153. TFIIA. 2 hits.
[Graphical view]
SMARTiSM01371. TFIIA. 1 hit.
[Graphical view]
SUPFAMiSSF47396. SSF47396. 1 hit.
SSF50784. SSF50784. 1 hit.
ProtoNetiSearch...

Entry informationi

Entry nameiTF2AA_HUMAN
AccessioniPrimary (citable) accession number: P52655
Secondary accession number(s): Q3KNQ9
Entry historyi
Integrated into UniProtKB/Swiss-Prot: October 1, 1996
Last sequence update: October 1, 1996
Last modified: November 30, 2016
This is version 173 of the entry and version 1 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 14
    Human chromosome 14: 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.