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P52657 (T2AG_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 130. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (4) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Interactions·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Transcription initiation factor IIA subunit 2
Alternative name(s):
General transcription factor IIA subunit 2
TFIIA p12 subunit
Short name=TFIIA-12
Short name=TFIIAS
Transcription initiation factor IIA gamma chain
Short name=TFIIA-gamma
Gene names
Name:GTF2A2
Synonyms:TF2A2
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length109 AA.
Sequence statusComplete.
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.11

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). Interacts with NCOA6 general coactivator By similarity. TFIIA forms a complex with TBP. Interacts with SV40 Large T antigen. Ref.9 Ref.10 Ref.11

Subcellular location

Nucleus.

Sequence similarities

Belongs to the TFIIA subunit 2 family.

Ontologies

Keywords
   Biological processHost-virus interaction
Transcription
Transcription regulation
   Cellular componentNucleus
   Technical term3D-structure
Complete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processRNA polymerase II transcriptional preinitiation complex assembly

Inferred from direct assay Ref.2PubMed 8626665. Source: BHF-UCL

gene expression

Traceable author statement. Source: Reactome

positive regulation of sequence-specific DNA binding transcription factor activity

Inferred from direct assay PubMed 8626665. Source: BHF-UCL

positive regulation of transcription from RNA polymerase II promoter

Inferred from direct assay Ref.2. Source: BHF-UCL

transcription elongation from RNA polymerase II promoter

Traceable author statement. Source: Reactome

transcription from RNA polymerase II promoter

Inferred from direct assay Ref.3Ref.1PubMed 8626665. Source: BHF-UCL

transcription initiation from RNA polymerase II promoter

Traceable author statement. Source: Reactome

viral process

Traceable author statement. Source: Reactome

   Cellular_componentcell junction

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 Ref.3Ref.2Ref.1. Source: BHF-UCL

   Molecular_functionTBP-class protein binding

Inferred from physical interaction Ref.3PubMed 8626665. Source: BHF-UCL

protein binding

Inferred from physical interaction Ref.3PubMed 8626665. Source: IntAct

protein heterodimerization activity

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

protein homodimerization activity

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

transcription coactivator activity

Inferred from direct assay Ref.2. Source: BHF-UCL

transcription factor binding

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

Complete GO annotation...

Binary interactions

With

Entry

#Exp.

IntAct

Notes

TBPP202262EBI-1045262,EBI-355371

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 109109Transcription initiation factor IIA subunit 2
PRO_0000194042

Secondary structure

............. 109
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
P52657 [UniParc].

Last modified October 1, 1996. Version 1.
Checksum: 938E7DC8B9982AE8

FASTA10912,457
        10         20         30         40         50         60 
MAYQLYRNTT LGNSLQESLD ELIQSQQITP QLALQVLLQF DKAINAALAQ RVRNRVNFRG 

        70         80         90        100 
SLNTYRFCDN VWTFVLNDVE FREVTELIKV DKVKIVACDG KNTGSNTTE 

« Hide

References

« Hide 'large scale' references
[1]"Reconstitution of human TFIIA activity from recombinant polypeptides: a role in TFIID-mediated transcription."
Sun X., Ma D., Sheldon M., Yeung K., Reinberg D.
Genes Dev. 8:2336-2348(1994) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
[2]"Molecular cloning of the small (gamma) subunit of human TFIIA reveals functions critical for activated transcription."
Ozer J., Moore P.A., Bolden A.H., Lee A., Rosen C.A., Lieberman P.M.
Genes Dev. 8:2324-2335(1994) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
[3]"Human general transcription factor TFIIA: characterization of a cDNA encoding the small subunit and requirement for basal and activated transcription."
Dejong J., Bernstein R., Roeder R.G.
Proc. Natl. Acad. Sci. U.S.A. 92:3313-3317(1995) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
[4]"Cloning of human full-length CDSs in BD Creator(TM) system donor vector."
Kalnine N., Chen X., Rolfs A., Halleck A., Hines L., Eisenstein S., Koundinya M., Raphael J., Moreira D., Kelley T., LaBaer J., Lin Y., Phelan M., Farmer A.
Submitted (MAY-2003) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
[5]"Cloning of human full open reading frames in Gateway(TM) system entry vector (pDONR201)."
Ebert L., Schick M., Neubert P., Schatten R., Henze S., Korn B.
Submitted (JUN-2004) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
[6]"Analysis of the DNA sequence and duplication history of human chromosome 15."
Zody M.C., Garber M., Sharpe T., Young S.K., Rowen L., O'Neill K., Whittaker C.A., Kamal M., Chang J.L., Cuomo C.A., Dewar K., FitzGerald M.G., Kodira C.D., Madan A., Qin S., Yang X., Abbasi N., Abouelleil A. expand/collapse author list , Arachchi H.M., Baradarani L., Birditt B., Bloom S., Bloom T., Borowsky M.L., Burke J., Butler J., Cook A., DeArellano K., DeCaprio D., Dorris L. III, Dors M., Eichler E.E., Engels R., Fahey J., Fleetwood P., Friedman C., Gearin G., Hall J.L., Hensley G., Johnson E., Jones C., Kamat A., Kaur A., Locke D.P., Madan A., Munson G., Jaffe D.B., Lui A., Macdonald P., Mauceli E., Naylor J.W., Nesbitt R., Nicol R., O'Leary S.B., Ratcliffe A., Rounsley S., She X., Sneddon K.M.B., Stewart S., Sougnez C., Stone S.M., Topham K., Vincent D., Wang S., Zimmer A.R., Birren B.W., Hood L., Lander E.S., Nusbaum C.
Nature 440:671-675(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[7]Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S., Turner R. expand/collapse author list , Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W., Venter J.C.
Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[8]"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].
Tissue: Lung.
[9]"Simian virus 40 large T antigen stabilizes the TATA-binding protein-TFIIA complex on the TATA element."
Damania B., Lieberman P., Alwine J.C.
Mol. Cell. Biol. 18:3926-3935(1998) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH SV40 LARGE T ANTIGEN.
[10]"A nuclear factor ASC-2, as a cancer-amplified transcriptional coactivator essential for ligand-dependent transactivation by nuclear receptors in vivo."
Lee S.-K., Anzick S.L., Choi J.-E., Bubendorf L., Guan X.-Y., Jung Y.-K., Kallioniemi O.-P., Kononen J., Trent J.M., Azorsa D., Jhun B.-H., Cheong J.H., Lee Y.C., Meltzer P.S., Lee J.W.
J. Biol. Chem. 274:34283-34293(1999) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH NCOA6.
[11]"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 GTF2A1 AND TBP.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
X81713 mRNA. Translation: CAA57357.1.
U14193 mRNA. Translation: AAA64951.1.
U21242 mRNA. Translation: AAB58247.1.
BT007362 mRNA. Translation: AAP36026.1.
CR542192 mRNA. Translation: CAG46989.1.
AC092755 Genomic DNA. No translation available.
CH471082 Genomic DNA. Translation: EAW77573.1.
BC000287 mRNA. Translation: AAH00287.1.
BC001919 mRNA. Translation: AAH01919.1.
CCDSCCDS10173.1.
PIRI38952.
RefSeqNP_004483.1. NM_004492.2.
XP_005254381.1. XM_005254324.1.
XP_005254382.1. XM_005254325.1.
UniGeneHs.512934.

3D structure databases

PDBe
RCSB-PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1NVPX-ray2.10D2-109[»]
ProteinModelPortalP52657.
SMRP52657. Positions 3-99.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid109213. 9 interactions.
IntActP52657. 2 interactions.
STRING9606.ENSP00000379372.

Chemistry

BindingDBP52657.

PTM databases

PhosphoSiteP52657.

Polymorphism databases

DMDM1729806.

Proteomic databases

MaxQBP52657.
PaxDbP52657.
PRIDEP52657.

Protocols and materials databases

DNASU2958.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000396060; ENSP00000379372; ENSG00000140307.
ENST00000396061; ENSP00000379373; ENSG00000140307.
ENST00000396063; ENSP00000379375; ENSG00000140307.
GeneID2958.
KEGGhsa:2958.
UCSCuc002agg.3. human.

Organism-specific databases

CTD2958.
GeneCardsGC15M059930.
HGNCHGNC:4647. GTF2A2.
HPAHPA056239.
MIM600519. gene.
neXtProtNX_P52657.
PharmGKBPA29034.
GenAtlasSearch...

Phylogenomic databases

eggNOGCOG5123.
HOGENOMHOG000167251.
HOVERGENHBG000826.
InParanoidP52657.
KOK03123.
OMACKNGDAI.
OrthoDBEOG7RFTKP.
PhylomeDBP52657.
TreeFamTF315131.

Enzyme and pathway databases

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

Gene expression databases

ArrayExpressP52657.
BgeeP52657.
CleanExHS_GTF2A2.
GenevestigatorP52657.

Family and domain databases

Gene3D1.10.287.190. 1 hit.
2.30.18.10. 1 hit.
InterProIPR009083. TFIIA_a-hlx.
IPR009088. TFIIA_b-brl.
IPR003194. TFIIA_gsu.
IPR015871. TFIIA_gsu_C.
IPR015872. TFIIA_gsu_N.
[Graphical view]
PANTHERPTHR10966. PTHR10966. 1 hit.
PfamPF02751. TFIIA_gamma_C. 1 hit.
PF02268. TFIIA_gamma_N. 1 hit.
[Graphical view]
PIRSFPIRSF009415. Hum_TFIIA_gamma. 1 hit.
ProDomPD009224. TFIIA_gsu_N. 1 hit.
[Graphical view] [Entries sharing at least one domain]
SUPFAMSSF47396. SSF47396. 1 hit.
SSF50784. SSF50784. 1 hit.
ProtoNetSearch...

Other

EvolutionaryTraceP52657.
GenomeRNAi2958.
NextBio11726.
PROP52657.
SOURCESearch...

Entry information

Entry nameT2AG_HUMAN
AccessionPrimary (citable) accession number: P52657
Secondary accession number(s): A8MYQ7, Q6FGB5
Entry history
Integrated into UniProtKB/Swiss-Prot: October 1, 1996
Last sequence update: October 1, 1996
Last modified: July 9, 2014
This is version 130 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 chromosome 15

Human chromosome 15: entries, gene names and cross-references to MIM