P52654 · TF2AA_DROME

Function

function

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.

GO annotations

all annotationsall molecular functionvirus receptor activitydna bindingrna bindingcytoskeletal motor activitycatalytic activitygtpase activitystructural molecule activitytransporter activitycytoskeletal protein bindinglipid bindingcyclase activityantioxidant activityoxidoreductase activitytransferase activityhydrolase activitylyase activityisomerase activityligase activityprotein tag activitycargo receptor activityhistone bindingprotein folding chaperonetranslation regulator activitynutrient reservoir activityreceptor ligand activitymolecular transducer activitymolecular adaptor activitytoxin activitycell adhesion mediator activitymolecular function regulator activityvirus coreceptor activitycatalytic activity, acting on a proteincatalytic activity, acting on dnacatalytic activity, acting on rnamolecular carrier activitytranscription regulator activitygeneral transcription initiation factor activitymolecular sensor activitymolecular sequestering activityatp-dependent activityother molecular functionall biological processmitotic cell cyclecytokinesiscytoplasmic translationimmune system processmuscle system processcirculatory system processrenal system processrespiratory system processcarbohydrate metabolic processgeneration of precursor metabolites and energydna replicationdna repairdna recombinationchromatin organizationdna-templated transcriptionregulation of dna-templated transcriptiontrna metabolic processprotein foldingprotein glycosylationamino acid metabolic processmodified amino acid metabolic processlipid metabolic processvitamin metabolic processsulfur compound metabolic processintracellular protein transportnucleocytoplasmic transportautophagyinflammatory responsemitochondrion organizationcytoskeleton organizationmicrotubule-based movementperoxisome organizationlysosome organizationchromosome segregationcell adhesionestablishment or maintenance of cell polarityprogrammed cell deathphotosynthesismrna metabolic processsnrna metabolic processvesicle-mediated transportreproductive processdigestive system processsignalingcell differentiationprotein catabolic processextracellular matrix organizationregulatory ncrna-mediated gene silencingtelomere organizationcell junction organizationwound healingribosome biogenesiscilium organizationanatomical structure developmentcell motilitynervous system processendocrine processprotein maturationtransmembrane transportnucleobase-containing small molecule metabolic processhepaticobiliary system processmembrane organizationprotein-containing complex assemblycell wall organization or biogenesisnitrogen cycle metabolic processprotein localization to plasma membranedefense response to other organismdetoxificationmeiotic nuclear divisionmitotic nuclear divisionmitochondrial gene expressioncarbohydrate derivative metabolic processother biological processall cellular componentnuclear chromosomeextracellular regionextracellular spacecell wallnucleusnuclear envelopenucleoplasmchromosomenucleolusmitochondrionlysosomeendosomevacuoleperoxisomeendoplasmic reticulumgolgi apparatuslipid dropletmicrotubule organizing centercytosolribosomecytoskeletonplasma membraneciliumplastidthylakoidexternal encapsulating structureextracellular matrixcytoplasmic vesicleorganelleother cellular component
Cell color indicative of number of GO terms
AspectTerm
Cellular Componentnucleus
Cellular Componenttranscription factor TFIIA complex
Molecular FunctionTBP-class protein binding
Molecular FunctionTFIID-class transcription factor complex binding
Biological Processtranscription by RNA polymerase II
Biological Processtranscription initiation at RNA polymerase II promoter

Keywords

Enzyme and pathway databases

Names & Taxonomy

Protein names

Gene names

    • Name
      TfIIA-L
    • ORF names
      CG5930

Organism names

  • Taxonomic identifier
  • Strain
    • Berkeley
  • Taxonomic lineage
    Eukaryota > Metazoa > Ecdysozoa > Arthropoda > Hexapoda > Insecta > Pterygota > Neoptera > Endopterygota > Diptera > Brachycera > Muscomorpha > Ephydroidea > Drosophilidae > Drosophila > Sophophora

Accessions

  • Primary accession
    P52654
  • Secondary accessions
    • Q8IMN7
    • Q8IMN8
    • Q95RK0
    • Q9VB56

Proteomes

Organism-specific databases

Subcellular Location

PTM/Processing

Features

Showing features for chain, modified residue.

TypeIDPosition(s)Description
ChainPRO_00000425911-262Transcription initiation factor IIA alpha chain
ChainPRO_00000425901-366Transcription initiation factor IIA subunit 1
ChainPRO_0000042592263-366Transcription initiation factor IIA beta chain
Modified residue265Phosphoserine; by TAF1
Modified residue306Phosphoserine; by TAF1

Post-translational modification

The precursor form (48 kDa) is cleaved to give rise to the alpha (30 kDa) and beta (20 kDa) subunits.

Keywords

Proteomic databases

Expression

Gene expression databases

Interaction

Subunit

Belongs to the TFIID complex which is composed of TATA binding protein (Tbp) and a number of TBP-associated factors (Tafs). TFIIA is a heterodimer of a unprocessed large subunit 1 and a small subunit gamma. It was originally believed to be a heterotrimer of an alpha (p30), a beta (p20) and a gamma subunit (p14). Interacts with Tbp. Taf4 interacts with TFIIA-L when TFIIA-L is in complex with Tbp.

Binary interactions

TypeEntry 1Entry 2Number of experimentsIntact
BINARY P52654TfIIA-S P526563EBI-132413, EBI-123680
BINARY P52654TfIIA-S-2 Q9W5B95EBI-132413, EBI-181168
View interactors in UniProtKB
View CPX-2248 in Complex Portal

Protein-protein interaction databases

Structure

Family & Domains

Features

Showing features for region, compositional bias.

TypeIDPosition(s)Description
Region56-82Disordered
Region133-162Disordered
Region257-317Disordered
Compositional bias264-317Acidic residues

Sequence similarities

Belongs to the TFIIA subunit 1 family.

Phylogenomic databases

Family and domain databases

Sequence & Isoforms

Align isoforms (3)
  • Sequence status
    Complete

This entry describes 3 isoforms produced by Alternative splicing.

P52654-1

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.

  • Length
    366
  • Mass (Da)
    39,268
  • Last updated
    2005-07-19 v2
  • Checksum
    73A3100332739643
MALCQTSVLKVYHAVIEDVITNVRDAFLDEGVDEQVLQEMKQVWRNKLLASKAVELSPDSGDGSHPPPIVANNPKSHKAANAKAKKAAAATAVTSHQHIGGNSSMSSLVGLKSSAGMAAGSGIRNGLVPIKQEVNSQNPPPLHPTSAASMMQKQQQAASSGQGSIPIVATLDPNRIMPVNITLPSPAGSASSESRVLTIQVPASALQENQLTQILTAHLISSIMSLPTTLASSVLQQHVNAALSSANHQKTLAAAKQLDGALDSSDEDESEESDDNIDNDDDDDLDKDDDEDAEHEDAAEEEPLNSEDDVTDEDSAEMFDTDNVIVCQYDKITRSRNKWKFYLKDGIMNMRGKDYVFQKSNGDAEW

P52654-2

  • Name
    B
  • See also
    sequence in UniParc or sequence clusters in UniRef
  • Differences from canonical

P52654-3

  • Name
    C
  • See also
    sequence in UniParc or sequence clusters in UniRef
  • Differences from canonical

Features

Showing features for alternative sequence, sequence conflict, compositional bias.

TypeIDPosition(s)Description
Alternative sequenceVSP_0147841-39in isoform C
Sequence conflict26in Ref. 1; AAB28821
Alternative sequenceVSP_01478575-77in isoform B and isoform C
Sequence conflict147in Ref. 1; AAB28821
Compositional bias264-317Acidic residues

Keywords

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
S66759
EMBL· GenBank· DDBJ
AAB28821.1
EMBL· GenBank· DDBJ
mRNA
AE014297
EMBL· GenBank· DDBJ
AAF56687.2
EMBL· GenBank· DDBJ
Genomic DNA
AE014297
EMBL· GenBank· DDBJ
AAN14105.1
EMBL· GenBank· DDBJ
Genomic DNA
AE014297
EMBL· GenBank· DDBJ
AAN14106.1
EMBL· GenBank· DDBJ
Genomic DNA
AY061325
EMBL· GenBank· DDBJ
AAL28873.1
EMBL· GenBank· DDBJ
mRNA

Genome annotation databases

Similar Proteins

Disclaimer

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