Skip Header

You are using a version of Internet Explorer that may not display all features of this website. Please upgrade to a modern browser.
Contribute Send feedback
Read comments (?) or add your own

P52655 (TF2AA_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 145. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (6) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Alt products·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended 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:

  1. Transcription initiation factor IIA alpha chain
    Alternative name(s):
    TFIIA p35 subunit
  2. Transcription initiation factor IIA beta chain
    Alternative name(s):
    TFIIA p19 subunit
Gene names
Name:GTF2A1
Synonyms:TF2A1
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length376 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

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. Ref.6 Ref.10

Subunit structure

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. Ref.6

Subcellular location

Nucleus.

Post-translational modification

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

Sequence similarities

Belongs to the TFIIA subunit 1 family.

Ontologies

Keywords
   Biological processTranscription
Transcription regulation
   Cellular componentNucleus
   Coding sequence diversityAlternative initiation
Polymorphism
   PTMAcetylation
Phosphoprotein
   Technical term3D-structure
Complete proteome
Direct protein sequencing
Reference proteome
Gene Ontology (GO)
   Biological_processgene expression

Traceable author statement. Source: Reactome

regulation of transcription, DNA-templated

Inferred from electronic annotation. Source: UniProtKB-KW

transcription elongation from RNA polymerase II promoter

Traceable author statement. Source: Reactome

transcription from RNA polymerase II promoter

Inferred from direct assay PubMed 7724559PubMed 7958900. Source: BHF-UCL

transcription initiation from RNA polymerase II promoter

Traceable author statement. Source: Reactome

viral process

Traceable author statement. Source: Reactome

   Cellular_componentcytoplasm

Inferred from direct assay. Source: HPA

nucleoplasm

Traceable author statement. Source: Reactome

nucleus

Inferred from direct assay. Source: HPA

transcription factor TFIIA complex

Inferred from direct assay PubMed 7724559. Source: BHF-UCL

   Molecular_functionDNA binding

Inferred from direct assay PubMed 7724559. Source: BHF-UCL

TBP-class protein binding

Inferred from physical interaction PubMed 7724559. Source: BHF-UCL

protein heterodimerization activity

Inferred from physical interaction PubMed 8626665. Source: BHF-UCL

transcription coactivator activity

Traceable author statement Ref.1. Source: ProtInc

transcription factor binding

Inferred from physical interaction PubMed 8626665. Source: BHF-UCL

Complete GO annotation...

Alternative products

This entry describes 2 isoforms produced by alternative initiation. [Align] [Select]
Isoform 42 kDa (identifier: P52655-1)

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.
Isoform 37 kDa (identifier: P52655-2)

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

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Initiator methionine11Removed Ref.11
Chain2 – 376375Transcription initiation factor IIA subunit 1
PRO_0000022481
Chain2 – 274273Transcription initiation factor IIA alpha chain
PRO_0000042593
Chain275 – 376102Transcription initiation factor IIA beta chain
PRO_0000042594

Regions

Compositional bias71 – 8010Poly-Gln
Compositional bias81 – 877Poly-His

Sites

Site274 – 2752Cleavage; by TASP1

Amino acid modifications

Modified residue21N-acetylalanine Ref.11 Ref.13
Modified residue2801Phosphoserine; by TAF1 Ref.7
Modified residue2811Phosphoserine; by TAF1 Ref.7
Modified residue3161Phosphoserine; by TAF1 Ref.7 Ref.9
Modified residue3211Phosphoserine; by TAF1 Ref.7 Ref.9

Natural variations

Alternative sequence1 – 3939Missing in isoform 37 kDa.
VSP_018798
Natural variant301L → V in a breast cancer sample; somatic mutation. Ref.14
VAR_035667
Natural variant1091A → P.
Corresponds to variant rs17111579 [ dbSNP | Ensembl ].
VAR_054043

Experimental info

Mutagenesis2701V → A: Slightly affects cleavage and yields elevated levels of the precursor. Ref.8
Mutagenesis2721Q → A: Abolishes cleavage. Ref.8
Mutagenesis2731V → A: Abolishes cleavage. Ref.8
Mutagenesis2741D → A: Abolishes cleavage. Ref.8
Mutagenesis2751G → A: Abolishes cleavage. Ref.8
Mutagenesis2761T → A: Does not affect cleavage. Ref.8
Mutagenesis2771G → A: Does not affect cleavage. Ref.8
Mutagenesis2781D → A: Significant reduction of cleavage. Ref.8
Mutagenesis2801S → A: Slightly affects cleavage, yields elevated levels of the precursor. Eliminates phosphorylation; when associated with A-281; A-316 and A-321. Ref.7 Ref.8
Mutagenesis2811S → A: Eliminates phosphorylation; when associated with A-280; A-316 and A-321. Ref.7
Mutagenesis2821E → A: Slightly affects cleavage and yields elevated levels of the precursor. Ref.8
Mutagenesis3161S → A: Strongly reduces phosphorylation; when associated with A-321. Eliminates phosphorylation; when associated with A-280; A-281 and A-321. Ref.7
Mutagenesis3211S → A: Strongly reduces phosphorylation; when associated with A-316. Eliminates phosphorylation; when associated with A-280; A-281 and A-316. Ref.7

Secondary structure

........... 376
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
Isoform 42 kDa [UniParc].

Last modified October 1, 1996. Version 1.
Checksum: 4BAE1853E7E89218

FASTA37641,514
        10         20         30         40         50         60 
MANSANTNTV PKLYRSVIED VINDVRDIFL DDGVDEQVLM ELKTLWENKL MQSRAVDGFH 

        70         80         90        100        110        120 
SEEQQLLLQV QQQHQPQQQQ HHHHHHHQQA QPQQTVPQQA QTQQVLIPAS QQATAPQVIV 

       130        140        150        160        170        180 
PDSKLIQHMN ASNMSAAATA ATLALPAGVT PVQQILTNSG QLLQVVRAAN GAQYIFQPQQ 

       190        200        210        220        230        240 
SVVLQQQVIP QMQPGGVQAP VIQQVLAPLP GGISPQTGVI IQPQQILFTG NKTQVIPTTV 

       250        260        270        280        290        300 
AAPTPAQAQI TATGQQQPQA QPAQTQAPLV LQVDGTGDTS SEEDEDEEED YDDDEEEDKE 

       310        320        330        340        350        360 
KDGAEDGQVE EEPLNSEDDV SDEEGQELFD TENVVVCQYD KIHRSKNKWK FHLKDGIMNL 

       370 
NGRDYIFSKA IGDAEW 

« Hide

Isoform 37 kDa [UniParc].

Checksum: 81D62BCC81399DE6
Show »

FASTA33737,152

References

« Hide 'large scale' references
[1]"Isolation of a cDNA encoding the largest subunit of TFIIA reveals functions important for activated transcription."
Ma D., Watanabe H., Mermelstein F., Admon A., Oguri K., Sun X., Wada T., Imai T., Shiroya T., Reinberg D., Handa H.
Genes Dev. 7:2246-2257(1993) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA], PARTIAL PROTEIN SEQUENCE.
[2]"A single cDNA, hTFIIA/alpha, encodes both the p35 and p19 subunits of human TFIIA."
Dejong J., Roeder R.G.
Genes Dev. 7:2220-2234(1993) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA], PARTIAL PROTEIN SEQUENCE.
[3]Watanabe H., Oguri K., Wada T., Imai T., Shiroya T., Handa H.
Submitted (JUN-1995) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
[4]"The DNA sequence and analysis of human chromosome 14."
Heilig R., Eckenberg R., Petit J.-L., Fonknechten N., Da Silva C., Cattolico L., Levy M., Barbe V., De Berardinis V., Ureta-Vidal A., Pelletier E., Vico V., Anthouard V., Rowen L., Madan A., Qin S., Sun H., Du H. expand/collapse author list , Pepin K., Artiguenave F., Robert C., Cruaud C., Bruels T., Jaillon O., Friedlander L., Samson G., Brottier P., Cure S., Segurens B., Aniere F., Samain S., Crespeau H., Abbasi N., Aiach N., Boscus D., Dickhoff R., Dors M., Dubois I., Friedman C., Gouyvenoux M., James R., Madan A., Mairey-Estrada B., Mangenot S., Martins N., Menard M., Oztas S., Ratcliffe A., Shaffer T., Trask B., Vacherie B., Bellemere C., Belser C., Besnard-Gonnet M., Bartol-Mavel D., Boutard M., Briez-Silla S., Combette S., Dufosse-Laurent V., Ferron C., Lechaplais C., Louesse C., Muselet D., Magdelenat G., Pateau E., Petit E., Sirvain-Trukniewicz P., Trybou A., Vega-Czarny N., Bataille E., Bluet E., Bordelais I., Dubois M., Dumont C., Guerin T., Haffray S., Hammadi R., Muanga J., Pellouin V., Robert D., Wunderle E., Gauguet G., Roy A., Sainte-Marthe L., Verdier J., Verdier-Discala C., Hillier L.W., Fulton L., McPherson J., Matsuda F., Wilson R., Scarpelli C., Gyapay G., Wincker P., Saurin W., Quetier F., Waterston R., Hood L., Weissenbach J.
Nature 421:601-607(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[5]"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
The MGC Project Team
Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
[6]"TAC, a TBP-sans-TAFs complex containing the unprocessed TFIIAalphabeta precursor and the TFIIAgamma subunit."
Mitsiou D.J., Stunnenberg H.G.
Mol. Cell 6:527-537(2000) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, SUBUNIT, IDENTIFICATION IN A COMPLEX WITH GTF2A2 AND TBP.
[7]"Taf(II) 250 phosphorylates human transcription factor IIA on serine residues important for TBP binding and transcription activity."
Solow S., Salunek M., Ryan R., Lieberman P.M.
J. Biol. Chem. 276:15886-15892(2001) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION AT SER-280; SER-281; SER-316 AND SER-321, MUTAGENESIS OF SER-280; SER-281; SER-316 AND SER-321.
[8]"Cleavage and proteasome-mediated degradation of the basal transcription factor TFIIA."
Hoiby T., Mitsiou D.J., Zhou H., Erdjument-Bromage H., Tempst P., Stunnenberg H.G.
EMBO J. 23:3083-3091(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: PROTEIN SEQUENCE OF 278-289, MUTAGENESIS OF VAL-270; GLN-272; VAL-273; ASP-274; GLY-275; THR-276; GLY-277; ASP-278; SER-280 AND GLU-282.
[9]"Global, in vivo, and site-specific phosphorylation dynamics in signaling networks."
Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P., Mann M.
Cell 127:635-648(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-316 AND SER-321, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[10]"Uncleaved TFIIA is a substrate for taspase 1 and active in transcription."
Zhou H., Spicuglia S., Hsieh J.J., Mitsiou D.J., Hoiby T., Veenstra G.J., Korsmeyer S.J., Stunnenberg H.G.
Mol. Cell. Biol. 26:2728-2735(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION OF THE GTF2A1 PRECURSOR, CLEAVAGE BY TASP1.
[11]"Lys-N and trypsin cover complementary parts of the phosphoproteome in a refined SCX-based approach."
Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S.
Anal. Chem. 81:4493-4501(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS], CLEAVAGE OF INITIATOR METHIONINE [LARGE SCALE ANALYSIS].
[12]"Initial characterization of the human central proteome."
Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.
BMC Syst. Biol. 5:17-17(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[13]"N-terminal acetylome analyses and functional insights of the N-terminal acetyltransferase NatB."
Van Damme P., Lasa M., Polevoda B., Gazquez C., Elosegui-Artola A., Kim D.S., De Juan-Pardo E., Demeyer K., Hole K., Larrea E., Timmerman E., Prieto J., Arnesen T., Sherman F., Gevaert K., Aldabe R.
Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012) [PubMed] [Europe PMC] [Abstract]
Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[14]"The consensus coding sequences of human breast and colorectal cancers."
Sjoeblom T., Jones S., Wood L.D., Parsons D.W., Lin J., Barber T.D., Mandelker D., Leary R.J., Ptak J., Silliman N., Szabo S., Buckhaults P., Farrell C., Meeh P., Markowitz S.D., Willis J., Dawson D., Willson J.K.V. expand/collapse author list , Gazdar A.F., Hartigan J., Wu L., Liu C., Parmigiani G., Park B.H., Bachman K.E., Papadopoulos N., Vogelstein B., Kinzler K.W., Velculescu V.E.
Science 314:268-274(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANT [LARGE SCALE ANALYSIS] VAL-30.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
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.
PIRA49077.
RefSeqNP_001265869.1. NM_001278940.1.
NP_056943.1. NM_015859.3.
NP_963889.1. NM_201595.2.
UniGeneHs.592334.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1NVPX-ray2.10B2-58[»]
C303-376[»]
ProteinModelPortalP52655.
SMRP52655. Positions 9-51, 330-376.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid109212. 47 interactions.
IntActP52655. 4 interactions.
STRING9606.ENSP00000298173.

PTM databases

PhosphoSiteP52655.

Polymorphism databases

DMDM1711663.

Proteomic databases

PaxDbP52655.
PRIDEP52655.

Protocols and materials databases

DNASU2957.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000434192; ENSP00000409492; ENSG00000165417. [P52655-2]
ENST00000553612; ENSP00000452454; ENSG00000165417. [P52655-1]
GeneID2957.
KEGGhsa:2957.
UCSCuc001xve.2. human. [P52655-1]

Organism-specific databases

CTD2957.
GeneCardsGC14M081646.
HGNCHGNC:4646. GTF2A1.
HPAHPA000869.
MIM600520. gene.
neXtProtNX_P52655.
PharmGKBPA29033.
GenAtlasSearch...

Phylogenomic databases

eggNOGCOG5149.
HOGENOMHOG000015236.
HOVERGENHBG052771.
InParanoidP52655.
KOK03122.
OMAHMSATGM.
OrthoDBEOG7KWSJM.
PhylomeDBP52655.
TreeFamTF350445.

Enzyme and pathway databases

ReactomeREACT_116125. Disease.
REACT_1788. Transcription.
REACT_71. Gene Expression.

Gene expression databases

ArrayExpressP52655.
BgeeP52655.
GenevestigatorP52655.

Family and domain databases

Gene3D1.10.287.100. 1 hit.
2.30.18.10. 1 hit.
InterProIPR009083. TFIIA_a-hlx.
IPR004855. TFIIA_asu/bsu.
IPR013028. TFIIA_asu_N.
IPR009088. TFIIA_b-brl.
[Graphical view]
PANTHERPTHR12694. PTHR12694. 1 hit.
PfamPF03153. TFIIA. 1 hit.
[Graphical view]
SUPFAMSSF47396. SSF47396. 1 hit.
SSF50784. SSF50784. 1 hit.
ProtoNetSearch...

Other

ChiTaRSGTF2A1. human.
EvolutionaryTraceP52655.
GeneWikiGTF2A1.
GenomeRNAi2957.
NextBio11720.
PMAP-CutDBP52655.
PROP52655.
SOURCESearch...

Entry information

Entry nameTF2AA_HUMAN
AccessionPrimary (citable) accession number: P52655
Secondary accession number(s): Q3KNQ9
Entry history
Integrated into UniProtKB/Swiss-Prot: October 1, 1996
Last sequence update: October 1, 1996
Last modified: April 16, 2014
This is version 145 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (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.

Relevant documents

SIMILARITY comments

Index of protein domains and families

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

Human polymorphisms and disease mutations

Index of human polymorphisms and disease mutations

Human entries with polymorphisms or disease mutations

List of human entries with polymorphisms or disease mutations

Human chromosome 14

Human chromosome 14: entries, gene names and cross-references to MIM