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P52655

- TF2AA_HUMAN

UniProt

P52655 - TF2AA_HUMAN

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Protein
Transcription initiation factor IIA subunit 1
Gene
GTF2A1, TF2A1
Organism
Homo sapiens (Human)
Status
Reviewed - 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

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sitei274 – 2752Cleavage; by TASP1

GO - Molecular functioni

  1. DNA binding Source: BHF-UCL
  2. TBP-class protein binding Source: BHF-UCL
  3. protein binding Source: UniProtKB
  4. protein heterodimerization activity Source: BHF-UCL
  5. transcription coactivator activity Source: ProtInc
  6. transcription factor binding Source: BHF-UCL

GO - Biological processi

  1. gene expression Source: Reactome
  2. regulation of transcription, DNA-templated Source: UniProtKB-KW
  3. transcription elongation from RNA polymerase II promoter Source: Reactome
  4. transcription from RNA polymerase II promoter Source: BHF-UCL
  5. transcription initiation from RNA polymerase II promoter Source: Reactome
  6. viral process Source: Reactome
Complete GO annotation...

Keywords - Biological processi

Transcription, Transcription regulation

Enzyme and pathway databases

ReactomeiREACT_1655. RNA Polymerase II Transcription Pre-Initiation And Promoter Opening.
REACT_1851. RNA Polymerase II Transcription Initiation.
REACT_2089. RNA Polymerase II Promoter Escape.
REACT_22107. RNA Polymerase II Pre-transcription Events.
REACT_6233. Transcription of the HIV genome.
REACT_6253. RNA Polymerase II HIV Promoter Escape.
REACT_6332. HIV Transcription Initiation.
REACT_834. RNA Polymerase II Transcription Initiation And Promoter Clearance.

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
ProteomesiUP000005640: Chromosome 14

Organism-specific databases

HGNCiHGNC:4646. GTF2A1.

Subcellular locationi

GO - Cellular componenti

  1. cytoplasm Source: HPA
  2. nucleoplasm Source: Reactome
  3. nucleus Source: HPA
  4. transcription factor TFIIA complex Source: BHF-UCL
Complete GO annotation...

Keywords - Cellular componenti

Nucleus

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi270 – 2701V → A: Slightly affects cleavage and yields elevated levels of the precursor. 1 Publication
Mutagenesisi272 – 2721Q → A: Abolishes cleavage. 1 Publication
Mutagenesisi273 – 2731V → A: Abolishes cleavage. 1 Publication
Mutagenesisi274 – 2741D → A: Abolishes cleavage. 1 Publication
Mutagenesisi275 – 2751G → A: Abolishes cleavage. 1 Publication
Mutagenesisi276 – 2761T → A: Does not affect cleavage. 1 Publication
Mutagenesisi277 – 2771G → A: Does not affect cleavage. 1 Publication
Mutagenesisi278 – 2781D → A: Significant reduction of cleavage. 1 Publication
Mutagenesisi280 – 2801S → A: Slightly affects cleavage, yields elevated levels of the precursor. Eliminates phosphorylation; when associated with A-281; A-316 and A-321. 2 Publications
Mutagenesisi281 – 2811S → A: Eliminates phosphorylation; when associated with A-280; A-316 and A-321. 1 Publication
Mutagenesisi282 – 2821E → A: Slightly affects cleavage and yields elevated levels of the precursor. 1 Publication
Mutagenesisi316 – 3161S → A: Strongly reduces phosphorylation; when associated with A-321. Eliminates phosphorylation; when associated with A-280; A-281 and A-321. 1 Publication
Mutagenesisi321 – 3211S → A: Strongly reduces phosphorylation; when associated with A-316. Eliminates phosphorylation; when associated with A-280; A-281 and A-316. 1 Publication

Organism-specific databases

PharmGKBiPA29033.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methioninei1 – 11Removed1 Publication
Chaini2 – 376375Transcription initiation factor IIA subunit 1
PRO_0000022481Add
BLAST
Chaini2 – 274273Transcription initiation factor IIA alpha chain
PRO_0000042593Add
BLAST
Chaini275 – 376102Transcription initiation factor IIA beta chain
PRO_0000042594Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei2 – 21N-acetylalanine2 Publications
Modified residuei280 – 2801Phosphoserine; by TAF11 Publication
Modified residuei281 – 2811Phosphoserine; by TAF11 Publication
Modified residuei316 – 3161Phosphoserine; by TAF12 Publications
Modified residuei321 – 3211Phosphoserine; by TAF12 Publications

Post-translational modificationi

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

Keywords - PTMi

Acetylation, Phosphoprotein

Proteomic databases

MaxQBiP52655.
PaxDbiP52655.
PRIDEiP52655.

PTM databases

PhosphoSiteiP52655.

Miscellaneous databases

PMAP-CutDBP52655.

Expressioni

Gene expression databases

ArrayExpressiP52655.
BgeeiP52655.
GenevestigatoriP52655.

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

Protein-protein interaction databases

BioGridi109212. 47 interactions.
IntActiP52655. 6 interactions.
STRINGi9606.ENSP00000298173.

Structurei

Secondary structure

Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi10 – 3223
Helixi36 – 5015
Beta strandi334 – 34512
Beta strandi348 – 36013
Beta strandi363 – 37513

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1NVPX-ray2.10B2-58[»]
C303-376[»]
ProteinModelPortaliP52655.
SMRiP52655. Positions 9-51, 330-376.

Miscellaneous databases

EvolutionaryTraceiP52655.

Family & Domainsi

Compositional bias

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Compositional biasi71 – 8010Poly-Gln
Compositional biasi81 – 877Poly-His

Sequence similaritiesi

Belongs to the TFIIA subunit 1 family.

Phylogenomic databases

eggNOGiCOG5149.
HOGENOMiHOG000015236.
HOVERGENiHBG052771.
InParanoidiP52655.
KOiK03122.
OMAiHMSATGM.
OrthoDBiEOG7KWSJM.
PhylomeDBiP52655.
TreeFamiTF350445.

Family and domain databases

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. 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. Align

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

MANSANTNTV PKLYRSVIED VINDVRDIFL DDGVDEQVLM ELKTLWENKL    50
MQSRAVDGFH SEEQQLLLQV QQQHQPQQQQ HHHHHHHQQA QPQQTVPQQA 100
QTQQVLIPAS QQATAPQVIV PDSKLIQHMN ASNMSAAATA ATLALPAGVT 150
PVQQILTNSG QLLQVVRAAN GAQYIFQPQQ SVVLQQQVIP QMQPGGVQAP 200
VIQQVLAPLP GGISPQTGVI IQPQQILFTG NKTQVIPTTV AAPTPAQAQI 250
TATGQQQPQA QPAQTQAPLV LQVDGTGDTS SEEDEDEEED YDDDEEEDKE 300
KDGAEDGQVE EEPLNSEDDV SDEEGQELFD TENVVVCQYD KIHRSKNKWK 350
FHLKDGIMNL NGRDYIFSKA IGDAEW 376
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)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti30 – 301L → V in a breast cancer sample; somatic mutation. 1 Publication
VAR_035667
Natural varianti109 – 1091A → P.
Corresponds to variant rs17111579 [ dbSNP | Ensembl ].
VAR_054043

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei1 – 3939Missing in isoform 37 kDa.
VSP_018798Add
BLAST

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
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.
UCSCiuc001xve.2. human. [P52655-1]

Polymorphism databases

DMDMi1711663.

Keywords - Coding sequence diversityi

Alternative initiation, Polymorphism

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
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 .
CCDSi CCDS9873.1. [P52655-1 ]
CCDS9874.1. [P52655-2 ]
PIRi A49077.
RefSeqi NP_001265869.1. NM_001278940.1.
NP_056943.1. NM_015859.3. [P52655-1 ]
NP_963889.1. NM_201595.2. [P52655-2 ]
UniGenei Hs.592334.

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
1NVP X-ray 2.10 B 2-58 [» ]
C 303-376 [» ]
ProteinModelPortali P52655.
SMRi P52655. Positions 9-51, 330-376.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 109212. 47 interactions.
IntActi P52655. 6 interactions.
STRINGi 9606.ENSP00000298173.

PTM databases

PhosphoSitei P52655.

Polymorphism databases

DMDMi 1711663.

Proteomic databases

MaxQBi P52655.
PaxDbi P52655.
PRIDEi P52655.

Protocols and materials databases

DNASUi 2957.
Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENST00000434192 ; ENSP00000409492 ; ENSG00000165417 . [P52655-2 ]
ENST00000553612 ; ENSP00000452454 ; ENSG00000165417 . [P52655-1 ]
GeneIDi 2957.
KEGGi hsa:2957.
UCSCi uc001xve.2. human. [P52655-1 ]

Organism-specific databases

CTDi 2957.
GeneCardsi GC14M081646.
HGNCi HGNC:4646. GTF2A1.
HPAi HPA000869.
MIMi 600520. gene.
neXtProti NX_P52655.
PharmGKBi PA29033.
GenAtlasi Search...

Phylogenomic databases

eggNOGi COG5149.
HOGENOMi HOG000015236.
HOVERGENi HBG052771.
InParanoidi P52655.
KOi K03122.
OMAi HMSATGM.
OrthoDBi EOG7KWSJM.
PhylomeDBi P52655.
TreeFami TF350445.

Enzyme and pathway databases

Reactomei REACT_1655. RNA Polymerase II Transcription Pre-Initiation And Promoter Opening.
REACT_1851. RNA Polymerase II Transcription Initiation.
REACT_2089. RNA Polymerase II Promoter Escape.
REACT_22107. RNA Polymerase II Pre-transcription Events.
REACT_6233. Transcription of the HIV genome.
REACT_6253. RNA Polymerase II HIV Promoter Escape.
REACT_6332. HIV Transcription Initiation.
REACT_834. RNA Polymerase II Transcription Initiation And Promoter Clearance.

Miscellaneous databases

ChiTaRSi GTF2A1. human.
EvolutionaryTracei P52655.
GeneWikii GTF2A1.
GenomeRNAii 2957.
NextBioi 11720.
PMAP-CutDB P52655.
PROi P52655.
SOURCEi Search...

Gene expression databases

ArrayExpressi P52655.
Bgeei P52655.
Genevestigatori P52655.

Family and domain databases

Gene3Di 1.10.287.100. 1 hit.
2.30.18.10. 1 hit.
InterProi IPR009083. TFIIA_a-hlx.
IPR004855. TFIIA_asu/bsu.
IPR013028. TFIIA_asu_N.
IPR009088. TFIIA_b-brl.
[Graphical view ]
PANTHERi PTHR12694. PTHR12694. 1 hit.
Pfami PF03153. TFIIA. 1 hit.
[Graphical view ]
SUPFAMi SSF47396. SSF47396. 1 hit.
SSF50784. SSF50784. 1 hit.
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  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.
    , 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. 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. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  13. Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  14. Cited for: VARIANT [LARGE SCALE ANALYSIS] VAL-30.

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: September 3, 2014
This is version 149 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

External Data

Dasty 3

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