GTF2A1

General transcription factor IIA, 1, 19/37kDa

PDB rendering based on 1nvp.

Available structures
PDB	1nvp

Identifiers

Symbols

GTF2A1; MGC129969; MGC129970; TF2A1; TFIIA

External IDs

OMIM: 600520 MGI: 1933277 HomoloGene: 56331 GeneCards: GTF2A1 Gene

Gene Ontology
Molecular function	• DNA binding • transcription coactivator activity • protein binding • transcription factor binding • TBP-class protein binding • protein heterodimerization activity
Cellular component	• nucleus • nucleoplasm • nucleoplasm • transcription factor TFIIA complex • nucleolus • cytoplasm
Biological process	• regulation of transcription, DNA-dependent • transcription from RNA polymerase II promoter • transcription from RNA polymerase II promoter • transcription initiation from RNA polymerase II promoter • transcription initiation from RNA polymerase II promoter • transcription elongation from RNA polymerase II promoter • gene expression • viral reproduction
Sources: Amigo / QuickGO

RNA expression pattern

More reference expression data

Orthologs

Species

Human

Mouse

RefSeq (mRNA)

RefSeq (protein)

Location (UCSC)

Chr 14:
81.65 – 81.69 Mb

Chr 12:
92.79 – 92.83 Mb

PubMed search

[1]

[2]

Transcription initiation factor IIA subunit 1 is a protein that in humans is encoded by the GTF2A1 gene.^[1]^[2]

1 Interactions
2 See also
3 References
4 Further reading

Interactions

GTF2A1 has been shown to interact with TATA binding protein^[3]^[4]^[5]^[6]^[7] and TBPL1.^[8]^[9]

References

^ DeJong J, Roeder RG (Dec 1993). "A single cDNA, hTFIIA/alpha, encodes both the p35 and p19 subunits of human TFIIA". Genes Dev 7 (11): 2220–34. doi:10.1101/gad.7.11.2220. PMID 8224848.
^ "Entrez Gene: GTF2A1 general transcription factor IIA, 1, 19/37kDa". http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=2957.
^ DeJong, J; Bernstein R, Roeder R G (Apr. 1995). "Human general transcription factor TFIIA: characterization of a cDNA encoding the small subunit and requirement for basal and activated transcription". Proc. Natl. Acad. Sci. U.S.A. (UNITED STATES) 92 (8): 3313–7. doi:10.1073/pnas.92.8.3313. ISSN 0027-8424. PMC 42156. PMID 7724559. http://www.pubmedcentral.nih.gov/articlerender.fcgi?tool=pmcentrez&artid=42156.
^ Langelier, M F; Forget D, Rojas A, Porlier Y, Burton Z F, Coulombe B (Oct. 2001). "Structural and functional interactions of transcription factor (TF) IIA with TFIIE and TFIIF in transcription initiation by RNA polymerase II". J. Biol. Chem. (United States) 276 (42): 38652–7. doi:10.1074/jbc.M106422200. ISSN 0021-9258. PMID 11509574.
^ Ozer, J; Mitsouras K, Zerby D, Carey M, Lieberman P M (Jun. 1998). "Transcription factor IIA derepresses TATA-binding protein (TBP)-associated factor inhibition of TBP-DNA binding". J. Biol. Chem. (UNITED STATES) 273 (23): 14293–300. doi:10.1074/jbc.273.23.14293. ISSN 0021-9258. PMID 9603936.
^ Solow, S; Salunek M, Ryan R, Lieberman P M (May. 2001). "Taf(II) 250 phosphorylates human transcription factor IIA on serine residues important for TBP binding and transcription activity". J. Biol. Chem. (United States) 276 (19): 15886–92. doi:10.1074/jbc.M009385200. ISSN 0021-9258. PMID 11278496.
^ Sun, X; Ma D, Sheldon M, Yeung K, Reinberg D (Oct. 1994). "Reconstitution of human TFIIA activity from recombinant polypeptides: a role in TFIID-mediated transcription". Genes Dev. (UNITED STATES) 8 (19): 2336–48. doi:10.1101/gad.8.19.2336. ISSN 0890-9369. PMID 7958900.
^ Ewing, Rob M; Chu Peter, Elisma Fred, Li Hongyan, Taylor Paul, Climie Shane, McBroom-Cerajewski Linda, Robinson Mark D, O'Connor Liam, Li Michael, Taylor Rod, Dharsee Moyez, Ho Yuen, Heilbut Adrian, Moore Lynda, Zhang Shudong, Ornatsky Olga, Bukhman Yury V, Ethier Martin, Sheng Yinglun, Vasilescu Julian, Abu-Farha Mohamed, Lambert Jean-Philippe, Duewel Henry S, Stewart Ian I, Kuehl Bonnie, Hogue Kelly, Colwill Karen, Gladwish Katharine, Muskat Brenda, Kinach Robert, Adams Sally-Lin, Moran Michael F, Morin Gregg B, Topaloglou Thodoros, Figeys Daniel (2007). "Large-scale mapping of human protein–protein interactions by mass spectrometry". Mol. Syst. Biol. (England) 3 (1): 89. doi:10.1038/msb4100134. PMC 1847948. PMID 17353931. http://www.pubmedcentral.nih.gov/articlerender.fcgi?tool=pmcentrez&artid=1847948.
^ Teichmann, M; Wang Z, Martinez E, Tjernberg A, Zhang D, Vollmer F, Chait B T, Roeder R G (Nov. 1999). "Human TATA-binding protein-related factor-2 (hTRF2) stably associates with hTFIIA in HeLa cells". Proc. Natl. Acad. Sci. U.S.A. (UNITED STATES) 96 (24): 13720–5. doi:10.1073/pnas.96.24.13720. ISSN 0027-8424. PMC 24131. PMID 10570139. http://www.pubmedcentral.nih.gov/articlerender.fcgi?tool=pmcentrez&artid=24131.

Ha I, Lane WS, Reinberg D (1991). "Cloning of a human gene encoding the general transcription initiation factor IIB". Nature 352 (6337): 689–95. doi:10.1038/352689a0. PMID 1876184.
DeJong J, Bernstein R, Roeder RG (1995). "Human general transcription factor TFIIA: characterization of a cDNA encoding the small subunit and requirement for basal and activated transcription". Proc. Natl. Acad. Sci. U.S.A. 92 (8): 3313–7. doi:10.1073/pnas.92.8.3313. PMC 42156. PMID 7724559. http://www.pubmedcentral.nih.gov/articlerender.fcgi?tool=pmcentrez&artid=42156.
Ozer J, Moore PA, Bolden AH, et al. (1994). "Molecular cloning of the small (gamma) subunit of human TFIIA reveals functions critical for activated transcription". Genes Dev. 8 (19): 2324–35. doi:10.1101/gad.8.19.2324. PMID 7958899.
Sun X, Ma D, Sheldon M, et al. (1994). "Reconstitution of human TFIIA activity from recombinant polypeptides: a role in TFIID-mediated transcription". Genes Dev. 8 (19): 2336–48. doi:10.1101/gad.8.19.2336. PMID 7958900.
Ge H, Roeder RG (1994). "The high mobility group protein HMG1 can reversibly inhibit class II gene transcription by interaction with the TATA-binding protein". J. Biol. Chem. 269 (25): 17136–40. PMID 8006019.
Ma D, Watanabe H, Mermelstein F, et al. (1993). "Isolation of a cDNA encoding the largest subunit of TFIIA reveals functions important for activated transcription". Genes Dev. 7 (11): 2246–57. doi:10.1101/gad.7.11.2246. PMID 8224850.
Tang H, Sun X, Reinberg D, Ebright RH (1996). "Protein-protein interactions in eukaryotic transcription initiation: structure of the preinitiation complex". Proc. Natl. Acad. Sci. U.S.A. 93 (3): 1119–24. doi:10.1073/pnas.93.3.1119. PMC 40041. PMID 8577725. http://www.pubmedcentral.nih.gov/articlerender.fcgi?tool=pmcentrez&artid=40041.
Kashanchi F, Khleif SN, Duvall JF, et al. (1996). "Interaction of human immunodeficiency virus type 1 Tat with a unique site of TFIID inhibits negative cofactor Dr1 and stabilizes the TFIID-TFIIA complex". J. Virol. 70 (8): 5503–10. PMC 190508. PMID 8764062. http://www.pubmedcentral.nih.gov/articlerender.fcgi?tool=pmcentrez&artid=190508.
Zhou Q, Sharp PA (1996). "Tat-SF1: cofactor for stimulation of transcriptional elongation by HIV-1 Tat". Science 274 (5287): 605–10. doi:10.1126/science.274.5287.605. PMID 8849451.
Bonaldo MF, Lennon G, Soares MB (1997). "Normalization and subtraction: two approaches to facilitate gene discovery". Genome Res. 6 (9): 791–806. doi:10.1101/gr.6.9.791. PMID 8889548.
Ozer J, Mitsouras K, Zerby D, et al. (1998). "Transcription factor IIA derepresses TATA-binding protein (TBP)-associated factor inhibition of TBP-DNA binding". J. Biol. Chem. 273 (23): 14293–300. doi:10.1074/jbc.273.23.14293. PMID 9603936.
Yokomori K, Verrijzer CP, Tjian R (1998). "An interplay between TATA box-binding protein and transcription factors IIE and IIA modulates DNA binding and transcription". Proc. Natl. Acad. Sci. U.S.A. 95 (12): 6722–7. doi:10.1073/pnas.95.12.6722. PMC 22611. PMID 9618479. http://www.pubmedcentral.nih.gov/articlerender.fcgi?tool=pmcentrez&artid=22611.
Na SY, Choi HS, Kim JW, et al. (1998). "Bcl3, an IkappaB protein, as a novel transcription coactivator of the retinoid X receptor". J. Biol. Chem. 273 (47): 30933–8. doi:10.1074/jbc.273.47.30933. PMID 9812988.
Upadhyaya AB, Lee SH, DeJong J (1999). "Identification of a general transcription factor TFIIAalpha/beta homolog selectively expressed in testis". J. Biol. Chem. 274 (25): 18040–8. doi:10.1074/jbc.274.25.18040. PMID 10364255.
Kim HJ, Yi JY, Sung HS, et al. (1999). "Activating Signal Cointegrator 1, a Novel Transcription Coactivator of Nuclear Receptors, and Its Cytosolic Localization under Conditions of Serum Deprivation". Mol. Cell. Biol. 19 (9): 6323–32. PMC 84603. PMID 10454579. http://www.pubmedcentral.nih.gov/articlerender.fcgi?tool=pmcentrez&artid=84603.
Lee SK, Anzick SL, Choi JE, et al. (1999). "A nuclear factor, ASC-2, as a cancer-amplified transcriptional coactivator essential for ligand-dependent transactivation by nuclear receptors in vivo". J. Biol. Chem. 274 (48): 34283–93. doi:10.1074/jbc.274.48.34283. PMID 10567404.
Teichmann M, Wang Z, Martinez E, et al. (2000). "Human TATA-binding protein-related factor-2 (hTRF2) stably associates with hTFIIA in HeLa cells". Proc. Natl. Acad. Sci. U.S.A. 96 (24): 13720–5. doi:10.1073/pnas.96.24.13720. PMC 24131. PMID 10570139. http://www.pubmedcentral.nih.gov/articlerender.fcgi?tool=pmcentrez&artid=24131.
Solow S, Salunek M, Ryan R, Lieberman PM (2001). "Taf(II) 250 phosphorylates human transcription factor IIA on serine residues important for TBP binding and transcription activity". J. Biol. Chem. 276 (19): 15886–92. doi:10.1074/jbc.M009385200. PMID 11278496.
Xing J, Sheppard HM, Corneillie SI, Liu X (2001). "p53 Stimulates TFIID-TFIIA-Promoter Complex Assembly, and p53-T Antigen Complex Inhibits TATA Binding Protein-TATA Interaction". Mol. Cell. Biol. 21 (11): 3652–61. doi:10.1128/MCB.21.11.3652-3661.2001. PMC 86992. PMID 11340159. http://www.pubmedcentral.nih.gov/articlerender.fcgi?tool=pmcentrez&artid=86992.

PDB gallery

1nvp: HUMAN TFIIA/TBP/DNA COMPLEX

Transcription factors and intracellular receptors

(1) Basic domains

(1.1) Basic leucine zipper (bZIP)	Activating transcription factor (AATF, 1, 2, 3, 4, 5, 6, 7) · AP-1 (c-Fos, FOSB, FOSL1, FOSL2, JDP2, c-Jun, JUNB, JUND) · BACH (1, 2) · BATF · BLZF1 · C/EBP (α, β, γ, δ, ε, ζ) · CREB (1, 3, L1) · CREM · DBP · DDIT3 · GABPA · HLF · MAF (B, F, G, K) · NFE (2, L1, L2, L3) · NFIL3 · NRL · NRF (1, 2, 3) · XBP1

(1.2) Basic helix-loop-helix (bHLH)	ATOH1 · AhR · AHRR · ARNT · ASCL1 · BHLHB2 · BMAL (ARNTL, ARNTL2) · CLOCK · EPAS1 · FIGLA · HAND (1, 2) · HES (5, 6) · HEY (1, 2, L) · HES1 · HIF (1A, 3A) · ID (1, 2, 3, 4) · LYL1 · MESP2 · MXD4 · MYCL1 · MYCN · Myogenic regulatory factors (MyoD, Myogenin, MYF5, MYF6) · Neurogenins (1, 2, 3) · NeuroD (1, 2) · NPAS (1, 2, 3) · OLIG (1, 2) · Pho4 · Scleraxis · SIM (1, 2) · TAL (1, 2) · Twist · USF1

(1.3) bHLH-ZIP	AP-4 · MAX · MITF · MNT · MLX · MXI1 · Myc · SREBP (1, 2)

(1.4) NF-1	NFI (A, B, C, X) · SMAD (R-SMAD (1, 2, 3, 5, 9) - I-SMAD (6, 7) - 4)

(1.5) RF-X	RFX (1, 2, 3, 4, 5, ANK)

(1.6) Basic helix-span-helix (bHSH)	AP-2 (α, β, γ, δ, ε)

(2) Zinc finger DNA-binding domains

(2.1) Nuclear receptor (Cys₄)	subfamily 1 (Thyroid hormone (α, β), CAR, FXR, LXR (α, β), PPAR (α, β/δ, γ), PXR, RAR (α, β, γ), ROR (α, β, γ), Rev-ErbA (α, β), VDR) subfamily 2 (COUP-TF (I, II), Ear-2, HNF4 (α, γ), PNR, RXR (α, β, γ), Testicular receptor (2, 4), TLX) subfamily 3 (Steroid hormone (Androgen, Estrogen (α, β), Glucocorticoid, Mineralocorticoid, Progesterone), Estrogen related (α, β, γ)) subfamily 4 NUR (NGFIB, NOR1, NURR1) · subfamily 5 (LRH-1, SF1) · subfamily 6 (GCNF) · subfamily 0 (DAX1, SHP)

(2.2) Other Cys₄	GATA (1, 2, 3, 4, 5, 6) · MTA (1, 2, 3) · TRPS1

(2.3) Cys₂His₂	General transcription factors (TFIIA, TFIIB, TFIID, TFIIE (1, 2), TFIIF (1, 2), TFIIH (1, 2, 4, 2I, 3A, 3C1, 3C2)) ATBF1 · BCL (6, 11A, 11B) · CTCF · E4F1 · EGR (1, 2, 3, 4) · ERV3 · GFI1 · GLI-Krüppel family (1, 2, 3, REST, S2, YY1) · HIC (1, 2) · HIVEP (1, 2, 3) · IKZF (1, 2, 3) · ILF (2, 3) · KLF (2, 3, 4, 5, 6, 7, 8, 9, 10, 11, 12, 13, 14, 15, 17) · MTF1 · MYT1 · OSR1 · PRDM9 · SALL (1, 2, 3, 4) · SP (1, 2, 4, 7, 8) · TSHZ3 · WT1 · Zbtb7 (7A, 7B) · ZBTB (16, 17, 20, 32, 33, 40) · zinc finger (3, 7, 9, 10, 19, 22, 24, 33B, 34, 35, 41, 43, 44, 51, 74, 143, 146, 148, 165, 202, 217, 219, 238, 239, 259, 267, 268, 281, 295, 300, 318, 330, 346, 350, 365, 366, 384, 423, 451, 452, 471, 593, 638, 644, 649, 655)

(2.4) Cys₆	HIVEP1

(2.5) Alternating composition	AIRE · DIDO1 · GRLF1 · ING (1, 2, 4) · JARID (1A, 1B, 1C, 1D, 2) · JMJD1B

(3) Helix-turn-helix domains

(3.1) Homeodomain	ARX · CDX (1, 2) · CRX · CUTL1 · DBX (1, 2) · DLX (3, 4, 5) · EMX2 · EN (1, 2) · FHL (1, 2, 3) · HESX1 · HHEX · HLX · Homeobox (A1, A2, A3, A4, A5, A7, A9, A10, A11, A13, B1, B2, B3, B4, B5, B6, B7, B8, B9, B13, C4, C5, C6, C8, C9, C10, C11, C12, C13, D1, D3, D4, D8, D9, D10, D11, D12, D13) · HOPX · IRX (1, 2, 3, 4, 5, 6, MKX) · LMX (1A, 1B) · MEIS (1, 2) · MEOX2 · MNX1 · MSX (1, 2) · NANOG · NKX (2-1, 2-2, 2-3, 2-5, 3-1, 3-2, 6-1, 6-2) · NOBOX · PBX (1, 2, 3) · PHF (1, 3, 6, 8, 10, 16, 17, 20, 21A) · PHOX (2A, 2B) · PITX (1, 2, 3) · POU domain (PIT-1, BRN-3: A, B, C, Octamer transcription factor: 1, 2, 3/4, 6, 7, 11) · OTX (1, 2) · PDX1 · SATB2 · SHOX2 · VAX1 · ZEB (1, 2)

(3.2) Paired box	PAX (1, 2, 3, 4, 5, 6, 7, 8, 9)

(3.3) Fork head / winged helix	E2F (1, 2, 3, 4, 5) · FOX proteins (A1, A2, A3, C1, C2, D3, D4, E1, E3, F1, G1, H1, I1, J1, J2, K1, K2, L2, M1, N1, N3, O1, O3, O4, P1, P2, P3, P4)

(3.4) Heat Shock Factors	HSF (1, 2, 4)

(3.5) Tryptophan clusters	ELF (2, 4, 5) · EGF · ELK (1, 3, 4) · ERF · ETS (1, 2, ERG, SPIB) · ETV (1, 4, 5, 6) · FLI1 · Interferon regulatory factors (1, 2, 3, 4, 5, 6, 7, 8) · MYB · MYBL2

(3.6) TEA domain	transcriptional enhancer factor (1, 2, 3, 4)

(4) β-Scaffold factors with minor groove contacts

(4.1) Rel homology region	NF-κB (NFKB1, NFKB2, REL, RELA, RELB) · NFAT (C1, C2, C3, C4, 5)

(4.2) STAT	STAT (1, 2, 3, 4, 5, 6)

(4.3) p53	p53 · TBX (1, 2, 3, 5, 19, 21, 22, Brachyury, TBR1, TBR2) · TP63

(4.4) MADS box	Mef2 (A, B, C, D) · SRF

(4.6) TATA binding proteins	TBP · TBPL1

(4.7) High-mobility group	BBX · HMGB (1, 2, 3, 4) · HMGN (1, 2, 3, 4) · HNF (1A, 1B) · LEF1 · SOX (1, 2, 3, 4, 5, 6, 8, 9, 10, 11, 12, 13, 14, 15, 18, 21) · SRY · SSRP1 · TCF (3, 4) · TOX (1, 2, 3, 4)

(4.10) Cold-shock domain	CSDA, YBX1

(4.11) Runt	CBF (CBFA2T2, CBFA2T3, RUNX1, RUNX2, RUNX3, RUNX1T1)

(0) Other transcription factors

(0.2) HMGI(Y)	HMGA (1, 2) · HBP1

(0.3) Pocket domain	Rb · RBL1 · RBL2

(0.5) AP-2/EREBP-related factors	Apetala 2 · EREBP · B3

(0.6) Miscellaneous	ARID (1A, 1B, 2, 3A, 3B, 4A) · CAP · IFI (16, 35) · MLL (2, 3, T1) · MNDA · NFY (A, B, C) · Rho/Sigma

see also transcription factor/coregulator deficiencies
B bsyn: dna (repl, cycl, reco, repr) · tscr (fact, tcrg, nucl, rnat, rept, ptts) · tltn (risu, pttl, nexn) · dnab, rnab/runp · stru (domn, 1°, 2°, 3°, 4°)

GTF2A1

Contents

Interactions

See also

References

Further reading