Reviewed, UniProtKB/Swiss-Prot P52655 (TF2AA_HUMAN)

Names and origin

Protein names

Recommended name:
    Transcription initiation factor IIA subunit 1
Alternative name(s):
    General transcription factor IIA subunit 1
    TFIIA-42
    TFIIAL
Cleaved into the following 2 chains:
    1- Recommended name:
            Transcription initiation factor IIA alpha chain
        Alternative name(s):
            TFIIA p35 subunit
    2- Recommended name:
            Transcription initiation factor IIA beta chain
        Alternative name(s):
            TFIIA p19 subunit

Gene names

Name:	GTF2A1
Synonyms:	TF2A1

Organism

Homo sapiens (Human) [Complete proteome]

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Primates › Haplorrhini › Catarrhini › Hominidae › Homo

Protein attributes

Sequence length	376 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence 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 proteosomal degradation.
Sequence similarities	Belongs to the TFIIA subunit 1 family.

Ontologies

Keywords
Biological process	Transcription Transcription regulation
Cellular component	Nucleus
Coding sequence diversity	Alternative initiation Polymorphism
PTM	Acetylation Phosphoprotein
Technical term	3D-structure Complete proteome Direct protein sequencing
Gene Ontology (GO)
Biological process	RNA elongation from RNA polymerase II promoter Inferred from Experiment. Source: Reactome general transcription from RNA polymerase II promoter Inferred from direct assay. Source: UniProtKB regulation of transcription Inferred from electronic annotation. Source: UniProtKB-KW transcription initiation from RNA polymerase II promoter Inferred from Experiment. Source: Reactome
Cellular component	cytoplasm Inferred from direct assay. Source: HPA nucleus Inferred from direct assay. Source: HPA transcription factor TFIIA complex Inferred from direct assay. Source: UniProtKB
Molecular function	DNA binding Inferred from direct assay. Source: UniProtKB TATA-binding protein binding Inferred from physical interaction. Source: UniProtKB general RNA polymerase II transcription factor activity Ref.1 Inferred from direct assay. Source: UniProtKB protein heterodimerization activity Inferred from physical interaction. Source: UniProtKB transcription coactivator activity Ref.1 Traceable author statement. Source: ProtInc
Complete GO annotation...

Binary interactions

With	Entry	#Exp.	IntAct	Notes
GTF2A2	P52657	1	EBI-389518,EBI-1045262
GTF2A2	P52657	1	EBI-1019093,EBI-1045262
TBP	P20226	1	EBI-1019093,EBI-355371
TBPL1	P62380	1	EBI-389518,EBI-716225

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 key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Initiator methionine

1

1

Removed

Chain

2 – 376

375

Transcription initiation factor IIA subunit 1

PRO_0000022481

Chain

2 – 274

273

Transcription initiation factor IIA alpha chain

PRO_0000042593

Chain

275 – 376

102

Transcription initiation factor IIA beta chain

PRO_0000042594

Regions

Compositional bias

71 – 80

10

Poly-Gln

Compositional bias

81 – 87

7

Poly-His

Sites

Site

274 – 275

2

Cleavage; by TASP1

Amino acid modifications

Modified residue

2

1

N-acetylalanine

Modified residue

12

1

N6-acetyllysine Ref.13

Modified residue

280

1

Phosphoserine; by TAF1 Ref.7

Modified residue

281

1

Phosphoserine; by TAF1 Ref.7

Modified residue

316

1

Phosphoserine; by TAF1 Ref.7 Ref.9

Modified residue

321

1

Phosphoserine; by TAF1 Ref.7 Ref.9

Natural variations

Alternative sequence

1 – 39

39

Missing in isoform 37 kDa.

VSP_018798

Natural variant

30

1

L → V in a breast cancer sample; somatic mutation. Ref.14

VAR_035667

Natural variant

109

1

A → P: dbSNP rs17111579.

VAR_054043

Experimental info

Mutagenesis

270

1

V → A: Slightly affects cleavage and yields elevated levels of the precursor. Ref.8

Mutagenesis

272

1

Q → A: Abolishes cleavage. Ref.8

Mutagenesis

273

1

V → A: Abolishes cleavage. Ref.8

Mutagenesis

274

1

D → A: Abolishes cleavage. Ref.8

Mutagenesis

275

1

G → A: Abolishes cleavage. Ref.8

Mutagenesis

276

1

T → A: Does not affect cleavage. Ref.8

Mutagenesis

277

1

G → A: Does not affect cleavage. Ref.8

Mutagenesis

278

1

D → A: Significant reduction of cleavage. Ref.8

Mutagenesis

280

1

S → 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

Mutagenesis

281

1

S → A: Eliminates phosphorylation; when associated with A-280; A-316 and A-321. Ref.7

Mutagenesis

282

1

E → A: Slightly affects cleavage and yields elevated levels of the precursor. Ref.8

Mutagenesis

316

1

S → A: Strongly reduces phosphorylation; when associated with A-321. Eliminates phosphorylation; when associated with A-280; A-281 and A-321. Ref.7

Mutagenesis

321

1

S → 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

1

.

.

.

.

.

.

.

.

.

.

.

376

Helix Strand Turn

Details...

Helix

10 – 32

23

Helix

36 – 50

15

Beta strand

334 – 345

12

Beta strand

348 – 360

13

Beta strand

363 – 375

13

Sequences

	Sequence		Length	Mass (Da)
	Isoform 42 kDa [UniParc]. Last modified October 1, 1996. Version 1. Checksum: 4BAE1853E7E89218	FASTA	376	41,514
	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
	Isoform 37 kDa. Checksum: 81D62BCC81399DE6	FASTA	337	37,152
	10 20 30 40 50 60 MELKTLWENK LMQSRAVDGF HSEEQQLLLQ VQQQHQPQQQ QHHHHHHHQQ AQPQQTVPQQ 70 80 90 100 110 120 AQTQQVLIPA SQQATAPQVI VPDSKLIQHM NASNMSAAAT AATLALPAGV TPVQQILTNS 130 140 150 160 170 180 GQLLQVVRAA NGAQYIFQPQ QSVVLQQQVI PQMQPGGVQA PVIQQVLAPL PGGISPQTGV 190 200 210 220 230 240 IIQPQQILFT GNKTQVIPTT VAAPTPAQAQ ITATGQQQPQ AQPAQTQAPL VLQVDGTGDT 250 260 270 280 290 300 SSEEDEDEEE DYDDDEEEDK EKDGAEDGQV EEEPLNSEDD VSDEEGQELF DTENVVVCQY 310 320 330 DKIHRSKNKW KFHLKDGIMN LNGRDYIFSK AIGDAEW

References

	« Hide 'large scale' referencesShow '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: 8224850] [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: 8224848] [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: 12508121] [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: 15489334] [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: 11030333] [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: 11278496] [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: 15257296] [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: 17081983] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-316 AND SER-321, MASS SPECTROMETRY. Tissue: Epithelium.
[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: 16537915] [Abstract] Cited for: FUNCTION OF THE GTF2A1 PRECURSOR, CLEAVAGE BY TASP1.
[11]	Colinge J., Superti-Furga G., Bennett K.L. Submitted (OCT-2008) to UniProtKB Cited for: IDENTIFICATION [LARGE SCALE ANALYSIS], MASS SPECTROMETRY.
[12]	"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: 19413330] [Abstract] Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, MASS SPECTROMETRY.
[13]	"Lysine acetylation targets protein complexes and co-regulates major cellular functions." Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T., Olsen J.V., Mann M. Science 325:834-840(2009) [PubMed: 19608861] [Abstract] Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-12, MASS SPECTROMETRY.
[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. , 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: 16959974] [Abstract] Cited for: VARIANT [LARGE SCALE ANALYSIS] VAL-30.
+	Additional computationally mapped references.

Cross-references

Sequence databases

EMBLGenBankDDBJ

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.

IPI

IPI00004350.
IPI00401787.

PIR

A49077.

RefSeq

NP_056943.1.
NP_963889.1.

UniGene

Hs.592334
Hs.593630

3D structure databases

PDBPDBe

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
1NVP	X-ray	2.10	B	2-58	[»]
			C	303-376	[»]

ModBase

Search...

Protein-protein interaction databases

IntAct

P52655. 5 interactions.

STRING

P52655.

PTM databases

PhosphoSite

P52655.

Proteomic databases

PRIDE

P52655.

Genome annotation databases

Ensembl

ENST00000298173; ENSP00000298173; ENSG00000165417; Homo sapiens. [Genome view]

GeneID

2957.

KEGG

hsa:2957.

UCSC

uc001xvf.1. human.
uc001xvg.1. human.

Organism-specific databases

CTD

2957.

GeneCards

GC14M080716.

H-InvDB

HIX0037748.

HGNC

HGNC:4646. GTF2A1.

HPA

HPA000869.

MIM

600520. gene.

PharmGKB

PA29033.

GenAtlas

Search...

Phylogenomic databases

HOGENOM

P52655.

HOVERGEN

P52655.

OMA

LMELKTX

OrthoDB

EOG9TB6XZ

Enzyme and pathway databases

Reactome

REACT_1788. Transcription.
REACT_6185. HIV Infection.
REACT_71. Gene Expression.

Gene expression databases

ArrayExpress

P52655.

Bgee

P52655.

Genevestigator

P52655.

GermOnline

ENSG00000165417. Homo sapiens.

Family and domain databases

InterPro

IPR009083. TFIIA_a-hlx.
IPR004855. TFIIA_asu/bsu.
IPR013028. TFIIA_asu_N.
IPR009088. TFIIA_b-brl.
[Graphical view]

Gene3D

G3DSA:1.10.287.100. TFIIA_asu_N. 1 hit.
G3DSA:2.30.18.10. TFIIA_betabarrel. 1 hit.

PANTHER

PTHR12694. TFIIA. 1 hit.

Pfam

PF03153. TFIIA. 1 hit.
[Graphical view]

ProtoNet

Search...

Other Resources

NextBio

11720.

PMAP-CutDB

P52655.

SOURCE

Search...

Entry information

Entry name

TF2AA_HUMAN

Accession

Primary (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:	November 24, 2009
This is version 98 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

HPI (Human Proteome Initiative)

Disclaimer

Any 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.