T2AG_HUMAN
ID T2AG_HUMAN Reviewed; 109 AA.
AC P52657; A8MYQ7; Q6FGB5;
DT 01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-1996, sequence version 1.
DT 03-AUG-2022, entry version 189.
DE RecName: Full=Transcription initiation factor IIA subunit 2;
DE AltName: Full=General transcription factor IIA subunit 2;
DE AltName: Full=TFIIA p12 subunit;
DE Short=TFIIA-12;
DE Short=TFIIAS;
DE AltName: Full=Transcription initiation factor IIA gamma chain;
DE Short=TFIIA-gamma;
GN Name=GTF2A2; Synonyms=TF2A2;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=7958900; DOI=10.1101/gad.8.19.2336;
RA Sun X., Ma D., Sheldon M., Yeung K., Reinberg D.;
RT "Reconstitution of human TFIIA activity from recombinant polypeptides: a
RT role in TFIID-mediated transcription.";
RL Genes Dev. 8:2336-2348(1994).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=7958899; DOI=10.1101/gad.8.19.2324;
RA Ozer J., Moore P.A., Bolden A.H., Lee A., Rosen C.A., Lieberman P.M.;
RT "Molecular cloning of the small (gamma) subunit of human TFIIA reveals
RT functions critical for activated transcription.";
RL Genes Dev. 8:2324-2335(1994).
RN [3]
RP NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=7724559; DOI=10.1073/pnas.92.8.3313;
RA Dejong J., Bernstein R., Roeder R.G.;
RT "Human general transcription factor TFIIA: characterization of a cDNA
RT encoding the small subunit and requirement for basal and activated
RT transcription.";
RL Proc. Natl. Acad. Sci. U.S.A. 92:3313-3317(1995).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RA Kalnine N., Chen X., Rolfs A., Halleck A., Hines L., Eisenstein S.,
RA Koundinya M., Raphael J., Moreira D., Kelley T., LaBaer J., Lin Y.,
RA Phelan M., Farmer A.;
RT "Cloning of human full-length CDSs in BD Creator(TM) system donor vector.";
RL Submitted (MAY-2003) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RA Ebert L., Schick M., Neubert P., Schatten R., Henze S., Korn B.;
RT "Cloning of human full open reading frames in Gateway(TM) system entry
RT vector (pDONR201).";
RL Submitted (JUN-2004) to the EMBL/GenBank/DDBJ databases.
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=16572171; DOI=10.1038/nature04601;
RA Zody M.C., Garber M., Sharpe T., Young S.K., Rowen L., O'Neill K.,
RA Whittaker C.A., Kamal M., Chang J.L., Cuomo C.A., Dewar K.,
RA FitzGerald M.G., Kodira C.D., Madan A., Qin S., Yang X., Abbasi N.,
RA Abouelleil A., Arachchi H.M., Baradarani L., Birditt B., Bloom S.,
RA Bloom T., Borowsky M.L., Burke J., Butler J., Cook A., DeArellano K.,
RA DeCaprio D., Dorris L. III, Dors M., Eichler E.E., Engels R., Fahey J.,
RA Fleetwood P., Friedman C., Gearin G., Hall J.L., Hensley G., Johnson E.,
RA Jones C., Kamat A., Kaur A., Locke D.P., Madan A., Munson G., Jaffe D.B.,
RA Lui A., Macdonald P., Mauceli E., Naylor J.W., Nesbitt R., Nicol R.,
RA O'Leary S.B., Ratcliffe A., Rounsley S., She X., Sneddon K.M.B.,
RA Stewart S., Sougnez C., Stone S.M., Topham K., Vincent D., Wang S.,
RA Zimmer A.R., Birren B.W., Hood L., Lander E.S., Nusbaum C.;
RT "Analysis of the DNA sequence and duplication history of human chromosome
RT 15.";
RL Nature 440:671-675(2006).
RN [7]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M.,
RA Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J.,
RA Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S.,
RA Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H.,
RA Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K.,
RA Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D.,
RA Hunkapiller M.W., Myers E.W., Venter J.C.;
RL Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN [8]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Lung;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [9]
RP INTERACTION WITH SV40 LARGE T ANTIGEN (MICROBIAL INFECTION).
RX PubMed=9632777; DOI=10.1128/mcb.18.7.3926;
RA Damania B., Lieberman P., Alwine J.C.;
RT "Simian virus 40 large T antigen stabilizes the TATA-binding protein-TFIIA
RT complex on the TATA element.";
RL Mol. Cell. Biol. 18:3926-3935(1998).
RN [10]
RP INTERACTION WITH NCOA6.
RX PubMed=10567404; DOI=10.1074/jbc.274.48.34283;
RA Lee S.-K., Anzick S.L., Choi J.-E., Bubendorf L., Guan X.-Y., Jung Y.-K.,
RA Kallioniemi O.-P., Kononen J., Trent J.M., Azorsa D., Jhun B.-H.,
RA Cheong J.H., Lee Y.C., Meltzer P.S., Lee J.W.;
RT "A nuclear factor ASC-2, as a cancer-amplified transcriptional coactivator
RT essential for ligand-dependent transactivation by nuclear receptors in
RT vivo.";
RL J. Biol. Chem. 274:34283-34293(1999).
RN [11]
RP INTERACTION WITH HSF1.
RX PubMed=11005381; DOI=10.1379/1466-1268(2000)005<0229:ptfhwt>2.0.co;2;
RA Yuan C.X., Gurley W.B.;
RT "Potential targets for HSF1 within the preinitiation complex.";
RL Cell Stress Chaperones 5:229-242(2000).
RN [12]
RP FUNCTION, SUBUNIT, AND IDENTIFICATION IN A COMPLEX WITH GTF2A1 AND TBP.
RX PubMed=11030333; DOI=10.1016/s1097-2765(00)00052-6;
RA Mitsiou D.J., Stunnenberg H.G.;
RT "TAC, a TBP-sans-TAFs complex containing the unprocessed TFIIAalphabeta
RT precursor and the TFIIAgamma subunit.";
RL Mol. Cell 6:527-537(2000).
CC -!- FUNCTION: TFIIA is a component of the transcription machinery of RNA
CC polymerase II and plays an important role in transcriptional
CC activation. TFIIA in a complex with TBP mediates transcriptional
CC activity. {ECO:0000269|PubMed:11030333}.
CC -!- SUBUNIT: TFIIA is a heterodimer of the large unprocessed subunit 1 and
CC a small subunit gamma (By similarity). It was originally believed to be
CC a heterotrimer of an alpha (p35), a beta (p19) and a gamma subunit
CC (p12) (By similarity). Interacts with NCOA6 general coactivator
CC (PubMed:10567404). TFIIA forms a complex with TBP (PubMed:11030333).
CC Interacts with HSF1 (via transactivation domain) (PubMed:11005381).
CC {ECO:0000250|UniProtKB:P52656, ECO:0000269|PubMed:10567404,
CC ECO:0000269|PubMed:11005381, ECO:0000269|PubMed:11030333}.
CC -!- SUBUNIT: (Microbial infection) Interacts with SV40 Large T antigen.
CC {ECO:0000269|PubMed:9632777}.
CC -!- INTERACTION:
CC P52657; P52655: GTF2A1; NbExp=12; IntAct=EBI-1045262, EBI-389518;
CC P52657; P20226: TBP; NbExp=2; IntAct=EBI-1045262, EBI-355371;
CC P52657; Q9C029: TRIM7; NbExp=3; IntAct=EBI-1045262, EBI-2813981;
CC -!- SUBCELLULAR LOCATION: Nucleus.
CC -!- SIMILARITY: Belongs to the TFIIA subunit 2 family. {ECO:0000305}.
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DR EMBL; X81713; CAA57357.1; -; mRNA.
DR EMBL; U14193; AAA64951.1; -; mRNA.
DR EMBL; U21242; AAB58247.1; -; mRNA.
DR EMBL; BT007362; AAP36026.1; -; mRNA.
DR EMBL; CR542192; CAG46989.1; -; mRNA.
DR EMBL; AC092755; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH471082; EAW77573.1; -; Genomic_DNA.
DR EMBL; BC000287; AAH00287.1; -; mRNA.
DR EMBL; BC001919; AAH01919.1; -; mRNA.
DR CCDS; CCDS10173.1; -.
DR PIR; I38952; I38952.
DR RefSeq; NP_001307858.1; NM_001320929.1.
DR RefSeq; NP_001307859.1; NM_001320930.1.
DR RefSeq; NP_004483.1; NM_004492.2.
DR PDB; 1NVP; X-ray; 2.10 A; D=2-109.
DR PDB; 5FUR; EM; 8.50 A; D=3-99.
DR PDB; 5IY6; EM; 7.20 A; O=1-109.
DR PDB; 5IY7; EM; 8.60 A; O=1-109.
DR PDB; 5IY8; EM; 7.90 A; O=1-109.
DR PDB; 5IY9; EM; 6.30 A; O=1-109.
DR PDB; 5IYA; EM; 5.40 A; O=1-109.
DR PDB; 5IYB; EM; 3.90 A; O=1-109.
DR PDB; 5IYC; EM; 3.90 A; O=1-109.
DR PDB; 5IYD; EM; 3.90 A; O=1-109.
DR PDB; 5M4S; X-ray; 2.38 A; A=2-103.
DR PDB; 6MZM; EM; 7.50 A; X=3-99.
DR PDB; 6O9L; EM; 7.20 A; O=1-109.
DR PDB; 7EDX; EM; 4.50 A; O=1-109.
DR PDB; 7EG7; EM; 6.20 A; O=1-109.
DR PDB; 7EG8; EM; 7.40 A; O=1-109.
DR PDB; 7EG9; EM; 3.70 A; O=1-109.
DR PDB; 7EGA; EM; 4.10 A; O=1-109.
DR PDB; 7EGB; EM; 3.30 A; O=1-109.
DR PDB; 7EGC; EM; 3.90 A; O=1-109.
DR PDB; 7EGD; EM; 6.75 A; O=1-109.
DR PDB; 7EGI; EM; 9.82 A; O=1-109.
DR PDB; 7EGJ; EM; 8.64 A; O=1-109.
DR PDB; 7ENA; EM; 4.07 A; DO=1-109.
DR PDB; 7ENC; EM; 4.13 A; DO=1-109.
DR PDB; 7LBM; EM; 4.80 A; N=1-109.
DR PDB; 7NVR; EM; 4.50 A; V=1-109.
DR PDB; 7NVS; EM; 2.80 A; V=1-109.
DR PDB; 7NVT; EM; 2.90 A; V=1-109.
DR PDB; 7NVU; EM; 2.50 A; V=1-109.
DR PDB; 7NVY; EM; 7.30 A; V=1-109.
DR PDB; 7NVZ; EM; 7.20 A; V=1-109.
DR PDB; 7NW0; EM; 6.60 A; V=1-109.
DR PDBsum; 1NVP; -.
DR PDBsum; 5FUR; -.
DR PDBsum; 5IY6; -.
DR PDBsum; 5IY7; -.
DR PDBsum; 5IY8; -.
DR PDBsum; 5IY9; -.
DR PDBsum; 5IYA; -.
DR PDBsum; 5IYB; -.
DR PDBsum; 5IYC; -.
DR PDBsum; 5IYD; -.
DR PDBsum; 5M4S; -.
DR PDBsum; 6MZM; -.
DR PDBsum; 6O9L; -.
DR PDBsum; 7EDX; -.
DR PDBsum; 7EG7; -.
DR PDBsum; 7EG8; -.
DR PDBsum; 7EG9; -.
DR PDBsum; 7EGA; -.
DR PDBsum; 7EGB; -.
DR PDBsum; 7EGC; -.
DR PDBsum; 7EGD; -.
DR PDBsum; 7EGI; -.
DR PDBsum; 7EGJ; -.
DR PDBsum; 7ENA; -.
DR PDBsum; 7ENC; -.
DR PDBsum; 7LBM; -.
DR PDBsum; 7NVR; -.
DR PDBsum; 7NVS; -.
DR PDBsum; 7NVT; -.
DR PDBsum; 7NVU; -.
DR PDBsum; 7NVY; -.
DR PDBsum; 7NVZ; -.
DR PDBsum; 7NW0; -.
DR AlphaFoldDB; P52657; -.
DR SMR; P52657; -.
DR BioGRID; 109213; 18.
DR ComplexPortal; CPX-519; Transcription factor complex TFIIA.
DR CORUM; P52657; -.
DR DIP; DIP-40648N; -.
DR IntAct; P52657; 7.
DR STRING; 9606.ENSP00000379372; -.
DR iPTMnet; P52657; -.
DR PhosphoSitePlus; P52657; -.
DR BioMuta; GTF2A2; -.
DR DMDM; 1729806; -.
DR EPD; P52657; -.
DR jPOST; P52657; -.
DR MassIVE; P52657; -.
DR MaxQB; P52657; -.
DR PaxDb; P52657; -.
DR PeptideAtlas; P52657; -.
DR PRIDE; P52657; -.
DR ProteomicsDB; 56501; -.
DR TopDownProteomics; P52657; -.
DR Antibodypedia; 25406; 103 antibodies from 21 providers.
DR DNASU; 2958; -.
DR Ensembl; ENST00000396060.7; ENSP00000379372.2; ENSG00000140307.11.
DR Ensembl; ENST00000396061.5; ENSP00000379373.1; ENSG00000140307.11.
DR Ensembl; ENST00000396063.5; ENSP00000379375.1; ENSG00000140307.11.
DR GeneID; 2958; -.
DR KEGG; hsa:2958; -.
DR MANE-Select; ENST00000396060.7; ENSP00000379372.2; NM_004492.3; NP_004483.1.
DR UCSC; uc002agg.3; human.
DR CTD; 2958; -.
DR DisGeNET; 2958; -.
DR GeneCards; GTF2A2; -.
DR HGNC; HGNC:4647; GTF2A2.
DR HPA; ENSG00000140307; Low tissue specificity.
DR MIM; 600519; gene.
DR neXtProt; NX_P52657; -.
DR OpenTargets; ENSG00000140307; -.
DR PharmGKB; PA29034; -.
DR VEuPathDB; HostDB:ENSG00000140307; -.
DR eggNOG; KOG3463; Eukaryota.
DR GeneTree; ENSGT00390000014572; -.
DR InParanoid; P52657; -.
DR OMA; QYYELYR; -.
DR OrthoDB; 1589933at2759; -.
DR PhylomeDB; P52657; -.
DR TreeFam; TF315131; -.
DR PathwayCommons; P52657; -.
DR Reactome; R-HSA-167161; HIV Transcription Initiation.
DR Reactome; R-HSA-167162; RNA Polymerase II HIV Promoter Escape.
DR Reactome; R-HSA-167172; Transcription of the HIV genome.
DR Reactome; R-HSA-674695; RNA Polymerase II Pre-transcription Events.
DR Reactome; R-HSA-6807505; RNA polymerase II transcribes snRNA genes.
DR Reactome; R-HSA-73776; RNA Polymerase II Promoter Escape.
DR Reactome; R-HSA-73779; RNA Polymerase II Transcription Pre-Initiation And Promoter Opening.
DR Reactome; R-HSA-75953; RNA Polymerase II Transcription Initiation.
DR Reactome; R-HSA-76042; RNA Polymerase II Transcription Initiation And Promoter Clearance.
DR Reactome; R-HSA-9018519; Estrogen-dependent gene expression.
DR SignaLink; P52657; -.
DR SIGNOR; P52657; -.
DR BioGRID-ORCS; 2958; 777 hits in 1064 CRISPR screens.
DR ChiTaRS; GTF2A2; human.
DR EvolutionaryTrace; P52657; -.
DR GenomeRNAi; 2958; -.
DR Pharos; P52657; Tbio.
DR PRO; PR:P52657; -.
DR Proteomes; UP000005640; Chromosome 15.
DR RNAct; P52657; protein.
DR Bgee; ENSG00000140307; Expressed in left testis and 206 other tissues.
DR ExpressionAtlas; P52657; baseline and differential.
DR Genevisible; P52657; HS.
DR GO; GO:0030054; C:cell junction; IDA:HPA.
DR GO; GO:0005654; C:nucleoplasm; IDA:HPA.
DR GO; GO:0005634; C:nucleus; IDA:ComplexPortal.
DR GO; GO:0005672; C:transcription factor TFIIA complex; IDA:BHF-UCL.
DR GO; GO:0005669; C:transcription factor TFIID complex; IDA:UniProtKB.
DR GO; GO:0046982; F:protein heterodimerization activity; IPI:BHF-UCL.
DR GO; GO:0042803; F:protein homodimerization activity; IPI:BHF-UCL.
DR GO; GO:0016251; F:RNA polymerase II general transcription initiation factor activity; IDA:ARUK-UCL.
DR GO; GO:0001091; F:RNA polymerase II general transcription initiation factor binding; IPI:BHF-UCL.
DR GO; GO:0061629; F:RNA polymerase II-specific DNA-binding transcription factor binding; IEA:Ensembl.
DR GO; GO:0017025; F:TBP-class protein binding; IPI:BHF-UCL.
DR GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; IDA:ComplexPortal.
DR GO; GO:0060261; P:positive regulation of transcription initiation from RNA polymerase II promoter; IDA:ComplexPortal.
DR GO; GO:0051123; P:RNA polymerase II preinitiation complex assembly; IDA:BHF-UCL.
DR GO; GO:0006366; P:transcription by RNA polymerase II; IDA:ARUK-UCL.
DR GO; GO:0006367; P:transcription initiation from RNA polymerase II promoter; IDA:BHF-UCL.
DR CDD; cd10014; TFIIA_gamma_C; 1.
DR CDD; cd10145; TFIIA_gamma_N; 1.
DR Gene3D; 1.10.287.190; -; 1.
DR Gene3D; 2.30.18.10; -; 1.
DR IDEAL; IID00556; -.
DR InterPro; IPR009083; TFIIA_a-hlx.
DR InterPro; IPR009088; TFIIA_b-brl.
DR InterPro; IPR003194; TFIIA_gsu.
DR InterPro; IPR015871; TFIIA_gsu_C.
DR InterPro; IPR015872; TFIIA_gsu_N.
DR PANTHER; PTHR10966; PTHR10966; 1.
DR Pfam; PF02751; TFIIA_gamma_C; 1.
DR Pfam; PF02268; TFIIA_gamma_N; 1.
DR PIRSF; PIRSF009415; Hum_TFIIA_gamma; 1.
DR SUPFAM; SSF50784; SSF50784; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Host-virus interaction; Nucleus; Reference proteome;
KW Transcription; Transcription regulation.
FT CHAIN 1..109
FT /note="Transcription initiation factor IIA subunit 2"
FT /id="PRO_0000194042"
FT HELIX 4..7
FT /evidence="ECO:0007829|PDB:1NVP"
FT HELIX 10..24
FT /evidence="ECO:0007829|PDB:1NVP"
FT HELIX 30..50
FT /evidence="ECO:0007829|PDB:1NVP"
FT STRAND 55..68
FT /evidence="ECO:0007829|PDB:1NVP"
FT STRAND 71..82
FT /evidence="ECO:0007829|PDB:1NVP"
FT STRAND 87..98
FT /evidence="ECO:0007829|PDB:1NVP"
SQ SEQUENCE 109 AA; 12457 MW; 938E7DC8B9982AE8 CRC64;
MAYQLYRNTT LGNSLQESLD ELIQSQQITP QLALQVLLQF DKAINAALAQ RVRNRVNFRG
SLNTYRFCDN VWTFVLNDVE FREVTELIKV DKVKIVACDG KNTGSNTTE
