ID   TF2AA_HUMAN             Reviewed;         376 AA.
AC   P52655; Q3KNQ9;
DT   01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-1996, sequence version 1.
DT   27-MAR-2024, entry version 218.
DE   RecName: Full=Transcription initiation factor IIA subunit 1;
DE   AltName: Full=General transcription factor IIA subunit 1;
DE   AltName: Full=TFIIAL;
DE   AltName: Full=Transcription initiation factor TFIIA 42 kDa subunit;
DE            Short=TFIIA-42;
DE   Contains:
DE     RecName: Full=Transcription initiation factor IIA alpha chain;
DE     AltName: Full=TFIIA p35 subunit;
DE   Contains:
DE     RecName: Full=Transcription initiation factor IIA beta chain;
DE     AltName: Full=TFIIA p19 subunit;
GN   Name=GTF2A1; Synonyms=TF2A1;
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], AND PARTIAL PROTEIN SEQUENCE.
RX   PubMed=8224850; DOI=10.1101/gad.7.11.2246;
RA   Ma D., Watanabe H., Mermelstein F., Admon A., Oguri K., Sun X., Wada T.,
RA   Imai T., Shiroya T., Reinberg D., Handa H.;
RT   "Isolation of a cDNA encoding the largest subunit of TFIIA reveals
RT   functions important for activated transcription.";
RL   Genes Dev. 7:2246-2257(1993).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [MRNA], AND PARTIAL PROTEIN SEQUENCE.
RX   PubMed=8224848; DOI=10.1101/gad.7.11.2220;
RA   Dejong J., Roeder R.G.;
RT   "A single cDNA, hTFIIA/alpha, encodes both the p35 and p19 subunits of
RT   human TFIIA.";
RL   Genes Dev. 7:2220-2234(1993).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RA   Watanabe H., Oguri K., Wada T., Imai T., Shiroya T., Handa H.;
RL   Submitted (JUN-1995) to the EMBL/GenBank/DDBJ databases.
RN   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=12508121; DOI=10.1038/nature01348;
RA   Heilig R., Eckenberg R., Petit J.-L., Fonknechten N., Da Silva C.,
RA   Cattolico L., Levy M., Barbe V., De Berardinis V., Ureta-Vidal A.,
RA   Pelletier E., Vico V., Anthouard V., Rowen L., Madan A., Qin S., Sun H.,
RA   Du H., Pepin K., Artiguenave F., Robert C., Cruaud C., Bruels T.,
RA   Jaillon O., Friedlander L., Samson G., Brottier P., Cure S., Segurens B.,
RA   Aniere F., Samain S., Crespeau H., Abbasi N., Aiach N., Boscus D.,
RA   Dickhoff R., Dors M., Dubois I., Friedman C., Gouyvenoux M., James R.,
RA   Madan A., Mairey-Estrada B., Mangenot S., Martins N., Menard M., Oztas S.,
RA   Ratcliffe A., Shaffer T., Trask B., Vacherie B., Bellemere C., Belser C.,
RA   Besnard-Gonnet M., Bartol-Mavel D., Boutard M., Briez-Silla S.,
RA   Combette S., Dufosse-Laurent V., Ferron C., Lechaplais C., Louesse C.,
RA   Muselet D., Magdelenat G., Pateau E., Petit E., Sirvain-Trukniewicz P.,
RA   Trybou A., Vega-Czarny N., Bataille E., Bluet E., Bordelais I., Dubois M.,
RA   Dumont C., Guerin T., Haffray S., Hammadi R., Muanga J., Pellouin V.,
RA   Robert D., Wunderle E., Gauguet G., Roy A., Sainte-Marthe L., Verdier J.,
RA   Verdier-Discala C., Hillier L.W., Fulton L., McPherson J., Matsuda F.,
RA   Wilson R., Scarpelli C., Gyapay G., Wincker P., Saurin W., Quetier F.,
RA   Waterston R., Hood L., Weissenbach J.;
RT   "The DNA sequence and analysis of human chromosome 14.";
RL   Nature 421:601-607(2003).
RN   [5]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
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   [6]
RP   FUNCTION, SUBUNIT, AND IDENTIFICATION IN A COMPLEX WITH GTF2A2 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).
RN   [7]
RP   PHOSPHORYLATION AT SER-280; SER-281; SER-316 AND SER-321, AND MUTAGENESIS
RP   OF SER-280; SER-281; SER-316 AND SER-321.
RX   PubMed=11278496; DOI=10.1074/jbc.m009385200;
RA   Solow S., Salunek M., Ryan R., Lieberman P.M.;
RT   "Taf(II) 250 phosphorylates human transcription factor IIA on serine
RT   residues important for TBP binding and transcription activity.";
RL   J. Biol. Chem. 276:15886-15892(2001).
RN   [8]
RP   PROTEIN SEQUENCE OF 278-289, AND MUTAGENESIS OF VAL-270; GLN-272; VAL-273;
RP   ASP-274; GLY-275; THR-276; GLY-277; ASP-278; SER-280 AND GLU-282.
RX   PubMed=15257296; DOI=10.1038/sj.emboj.7600304;
RA   Hoiby T., Mitsiou D.J., Zhou H., Erdjument-Bromage H., Tempst P.,
RA   Stunnenberg H.G.;
RT   "Cleavage and proteasome-mediated degradation of the basal transcription
RT   factor TFIIA.";
RL   EMBO J. 23:3083-3091(2004).
RN   [9]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-316 AND SER-321, AND
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Cervix carcinoma;
RX   PubMed=17081983; DOI=10.1016/j.cell.2006.09.026;
RA   Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P., Mann M.;
RT   "Global, in vivo, and site-specific phosphorylation dynamics in signaling
RT   networks.";
RL   Cell 127:635-648(2006).
RN   [10]
RP   FUNCTION OF THE GTF2A1 PRECURSOR, AND CLEAVAGE BY TASP1.
RX   PubMed=16537915; DOI=10.1128/mcb.26.7.2728-2735.2006;
RA   Zhou H., Spicuglia S., Hsieh J.J., Mitsiou D.J., Hoiby T., Veenstra G.J.,
RA   Korsmeyer S.J., Stunnenberg H.G.;
RT   "Uncleaved TFIIA is a substrate for taspase 1 and active in
RT   transcription.";
RL   Mol. Cell. Biol. 26:2728-2735(2006).
RN   [11]
RP   ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, CLEAVAGE OF INITIATOR
RP   METHIONINE [LARGE SCALE ANALYSIS], AND IDENTIFICATION BY MASS SPECTROMETRY
RP   [LARGE SCALE ANALYSIS].
RX   PubMed=19413330; DOI=10.1021/ac9004309;
RA   Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S.;
RT   "Lys-N and trypsin cover complementary parts of the phosphoproteome in a
RT   refined SCX-based approach.";
RL   Anal. Chem. 81:4493-4501(2009).
RN   [12]
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX   PubMed=21269460; DOI=10.1186/1752-0509-5-17;
RA   Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T.,
RA   Bennett K.L., Superti-Furga G., Colinge J.;
RT   "Initial characterization of the human central proteome.";
RL   BMC Syst. Biol. 5:17-17(2011).
RN   [13]
RP   ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, CLEAVAGE OF INITIATOR
RP   METHIONINE [LARGE SCALE ANALYSIS], AND IDENTIFICATION BY MASS SPECTROMETRY
RP   [LARGE SCALE ANALYSIS].
RX   PubMed=22814378; DOI=10.1073/pnas.1210303109;
RA   Van Damme P., Lasa M., Polevoda B., Gazquez C., Elosegui-Artola A.,
RA   Kim D.S., De Juan-Pardo E., Demeyer K., Hole K., Larrea E., Timmerman E.,
RA   Prieto J., Arnesen T., Sherman F., Gevaert K., Aldabe R.;
RT   "N-terminal acetylome analyses and functional insights of the N-terminal
RT   acetyltransferase NatB.";
RL   Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012).
RN   [14]
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Liver;
RX   PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014;
RA   Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L.,
RA   Ye M., Zou H.;
RT   "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver
RT   phosphoproteome.";
RL   J. Proteomics 96:253-262(2014).
RN   [15]
RP   STRUCTURE BY ELECTRON MICROSCOPY (3.90 ANGSTROMS) IN COMPLEX WITH PROMOTER
RP   DNA, AND SUBUNIT.
RX   PubMed=27193682; DOI=10.1038/nature17970;
RA   He Y., Yan C., Fang J., Inouye C., Tjian R., Ivanov I., Nogales E.;
RT   "Near-atomic resolution visualization of human transcription promoter
RT   opening.";
RL   Nature 533:359-365(2016).
RN   [16]
RP   VARIANT [LARGE SCALE ANALYSIS] VAL-30.
RX   PubMed=16959974; DOI=10.1126/science.1133427;
RA   Sjoeblom T., Jones S., Wood L.D., Parsons D.W., Lin J., Barber T.D.,
RA   Mandelker D., Leary R.J., Ptak J., Silliman N., Szabo S., Buckhaults P.,
RA   Farrell C., Meeh P., Markowitz S.D., Willis J., Dawson D., Willson J.K.V.,
RA   Gazdar A.F., Hartigan J., Wu L., Liu C., Parmigiani G., Park B.H.,
RA   Bachman K.E., Papadopoulos N., Vogelstein B., Kinzler K.W.,
RA   Velculescu V.E.;
RT   "The consensus coding sequences of human breast and colorectal cancers.";
RL   Science 314:268-274(2006).
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, ECO:0000269|PubMed:16537915}.
CC   -!- SUBUNIT: TFIIA is a heterodimer of the large unprocessed subunit 1 and
CC       a small subunit gamma. It was originally believed to be a heterotrimer
CC       of an alpha (p35), a beta (p19) and a gamma subunit (p12). TFIIA forms
CC       a complex with TBP. Part of TBP-based Pol II pre-initiation complex
CC       (PIC), in which Pol II core assembles with general transcription
CC       factors and other specific initiation factors including GTF2E1, GTF2E2,
CC       GTF2F1, GTF2F2, TCEA1, ERCC2, ERCC3, GTF2H2, GTF2H3, GTF2H4, GTF2H5,
CC       GTF2A1, GTF2A2, GTF2B and TBP; this large multi-subunit PIC complex
CC       mediates DNA unwinding and targets Pol II core to the transcription
CC       start site where the first phosphodiester bond forms.
CC       {ECO:0000269|PubMed:11030333, ECO:0000269|PubMed:27193682}.
CC   -!- INTERACTION:
CC       P52655; Q96CA5: BIRC7; NbExp=3; IntAct=EBI-389518, EBI-517623;
CC       P52655; O75460-2: ERN1; NbExp=3; IntAct=EBI-389518, EBI-25852368;
CC       P52655; P22607: FGFR3; NbExp=3; IntAct=EBI-389518, EBI-348399;
CC       P52655; Q0VDC6: FKBP1A; NbExp=3; IntAct=EBI-389518, EBI-10226858;
CC       P52655; P52657: GTF2A2; NbExp=12; IntAct=EBI-389518, EBI-1045262;
CC       P52655; P01112: HRAS; NbExp=3; IntAct=EBI-389518, EBI-350145;
CC       P52655; P23511: NFYA; NbExp=3; IntAct=EBI-389518, EBI-389739;
CC       P52655; P23511-2: NFYA; NbExp=3; IntAct=EBI-389518, EBI-11061759;
CC       P52655; D3DTS7: PMP22; NbExp=3; IntAct=EBI-389518, EBI-25882629;
CC       P52655; P86480: PRR20D; NbExp=3; IntAct=EBI-389518, EBI-12754095;
CC       P52655; P62333: PSMC6; NbExp=3; IntAct=EBI-389518, EBI-357669;
CC       P52655; Q02446: SP4; NbExp=3; IntAct=EBI-389518, EBI-10198587;
CC       P52655; P20226: TBP; NbExp=2; IntAct=EBI-389518, EBI-355371;
CC       P52655; P62380: TBPL1; NbExp=5; IntAct=EBI-389518, EBI-716225;
CC   -!- SUBCELLULAR LOCATION: Nucleus.
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative initiation; Named isoforms=2;
CC       Name=42 kDa;
CC         IsoId=P52655-1; Sequence=Displayed;
CC       Name=37 kDa;
CC         IsoId=P52655-2; Sequence=VSP_018798;
CC   -!- PTM: The alpha and beta subunits are postranslationally produced from
CC       the precursor form by TASP1. The cleavage promotes proteasomal
CC       degradation. {ECO:0000269|PubMed:16537915}.
CC   -!- SIMILARITY: Belongs to the TFIIA subunit 1 family. {ECO:0000305}.
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DR   EMBL; X75383; CAA53151.1; -; mRNA.
DR   EMBL; X75383; CAA53152.1; -; mRNA.
DR   EMBL; X77225; CAA54442.1; -; mRNA.
DR   EMBL; D14887; BAA03604.1; -; mRNA.
DR   EMBL; D14886; BAA03603.1; -; mRNA.
DR   EMBL; AC010582; AAF26776.1; -; Genomic_DNA.
DR   EMBL; BC107155; AAI07156.1; -; mRNA.
DR   EMBL; BC107156; AAI07157.1; -; mRNA.
DR   CCDS; CCDS9873.1; -. [P52655-1]
DR   CCDS; CCDS9874.1; -. [P52655-2]
DR   PIR; A49077; A49077.
DR   RefSeq; NP_001265869.1; NM_001278940.1.
DR   RefSeq; NP_056943.1; NM_015859.3. [P52655-1]
DR   RefSeq; NP_963889.1; NM_201595.2. [P52655-2]
DR   PDB; 1NVP; X-ray; 2.10 A; B=2-58, C=303-376.
DR   PDB; 5FUR; EM; 8.50 A; B=9-51, C=330-376.
DR   PDB; 5IY6; EM; 7.20 A; N=1-376.
DR   PDB; 5IY7; EM; 8.60 A; N=1-376.
DR   PDB; 5IY8; EM; 7.90 A; N=1-376.
DR   PDB; 5IY9; EM; 6.30 A; N=1-376.
DR   PDB; 5IYA; EM; 5.40 A; N=1-376.
DR   PDB; 5IYB; EM; 3.90 A; N=1-376.
DR   PDB; 5IYC; EM; 3.90 A; N=1-376.
DR   PDB; 5IYD; EM; 3.90 A; N=1-376.
DR   PDB; 5M4S; X-ray; 2.38 A; A=2-58, A=328-376.
DR   PDB; 6MZM; EM; 7.50 A; W=9-376.
DR   PDB; 6O9L; EM; 7.20 A; N=1-376.
DR   PDB; 7EDX; EM; 4.50 A; Q=1-376.
DR   PDB; 7EG7; EM; 6.20 A; Q=1-376.
DR   PDB; 7EG8; EM; 7.40 A; Q=1-376.
DR   PDB; 7EG9; EM; 3.70 A; Q=1-376.
DR   PDB; 7EGA; EM; 4.10 A; Q=1-376.
DR   PDB; 7EGB; EM; 3.30 A; Q=1-376.
DR   PDB; 7EGC; EM; 3.90 A; Q=1-376.
DR   PDB; 7EGD; EM; 6.75 A; Q=1-376.
DR   PDB; 7EGI; EM; 9.82 A; Q=1-376.
DR   PDB; 7EGJ; EM; 8.64 A; Q=1-376.
DR   PDB; 7LBM; EM; 4.80 A; M=1-376.
DR   PDB; 7NVR; EM; 4.50 A; U=1-376.
DR   PDB; 7NVS; EM; 2.80 A; U=1-376.
DR   PDB; 7NVT; EM; 2.90 A; U=1-376.
DR   PDB; 7NVU; EM; 2.50 A; U=1-376.
DR   PDB; 7NVY; EM; 7.30 A; U=1-376.
DR   PDB; 7NVZ; EM; 7.20 A; U=1-376.
DR   PDB; 7NW0; EM; 6.60 A; U=1-376.
DR   PDB; 7ZWC; EM; 3.20 A; U=1-376.
DR   PDB; 7ZWD; EM; 3.00 A; U=1-376.
DR   PDB; 7ZX7; EM; 3.40 A; U=1-376.
DR   PDB; 7ZX8; EM; 3.00 A; U=1-376.
DR   PDB; 7ZXE; EM; 3.50 A; U=1-376.
DR   PDB; 8BVW; EM; 4.00 A; U=1-376.
DR   PDB; 8BYQ; EM; 4.10 A; U=1-376.
DR   PDB; 8BZ1; EM; 3.80 A; U=1-376.
DR   PDB; 8GXQ; EM; 5.04 A; DQ=1-376.
DR   PDB; 8GXS; EM; 4.16 A; DQ=1-376.
DR   PDB; 8WAK; EM; 5.47 A; Q=1-376.
DR   PDB; 8WAL; EM; 8.52 A; Q=1-376.
DR   PDB; 8WAN; EM; 6.07 A; Q=1-376.
DR   PDB; 8WAO; EM; 6.40 A; Q=1-376.
DR   PDB; 8WAP; EM; 5.85 A; Q=1-376.
DR   PDB; 8WAQ; EM; 6.29 A; Q=1-376.
DR   PDB; 8WAR; EM; 7.20 A; Q=1-376.
DR   PDB; 8WAS; EM; 6.13 A; Q=1-376.
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; 7LBM; -.
DR   PDBsum; 7NVR; -.
DR   PDBsum; 7NVS; -.
DR   PDBsum; 7NVT; -.
DR   PDBsum; 7NVU; -.
DR   PDBsum; 7NVY; -.
DR   PDBsum; 7NVZ; -.
DR   PDBsum; 7NW0; -.
DR   PDBsum; 7ZWC; -.
DR   PDBsum; 7ZWD; -.
DR   PDBsum; 7ZX7; -.
DR   PDBsum; 7ZX8; -.
DR   PDBsum; 7ZXE; -.
DR   PDBsum; 8BVW; -.
DR   PDBsum; 8BYQ; -.
DR   PDBsum; 8BZ1; -.
DR   PDBsum; 8GXQ; -.
DR   PDBsum; 8GXS; -.
DR   PDBsum; 8WAK; -.
DR   PDBsum; 8WAL; -.
DR   PDBsum; 8WAN; -.
DR   PDBsum; 8WAO; -.
DR   PDBsum; 8WAP; -.
DR   PDBsum; 8WAQ; -.
DR   PDBsum; 8WAR; -.
DR   PDBsum; 8WAS; -.
DR   AlphaFoldDB; P52655; -.
DR   EMDB; EMD-12610; -.
DR   EMDB; EMD-12611; -.
DR   EMDB; EMD-12612; -.
DR   EMDB; EMD-12613; -.
DR   EMDB; EMD-12617; -.
DR   EMDB; EMD-12618; -.
DR   EMDB; EMD-12619; -.
DR   EMDB; EMD-14996; -.
DR   EMDB; EMD-14997; -.
DR   EMDB; EMD-15006; -.
DR   EMDB; EMD-15007; -.
DR   EMDB; EMD-15009; -.
DR   EMDB; EMD-16274; -.
DR   EMDB; EMD-16331; -.
DR   EMDB; EMD-16335; -.
DR   EMDB; EMD-23255; -.
DR   EMDB; EMD-31075; -.
DR   EMDB; EMD-31107; -.
DR   EMDB; EMD-31108; -.
DR   EMDB; EMD-31109; -.
DR   EMDB; EMD-31110; -.
DR   EMDB; EMD-31111; -.
DR   EMDB; EMD-31112; -.
DR   EMDB; EMD-31113; -.
DR   EMDB; EMD-31118; -.
DR   EMDB; EMD-31119; -.
DR   EMDB; EMD-3305; -.
DR   EMDB; EMD-34359; -.
DR   EMDB; EMD-34360; -.
DR   EMDB; EMD-8132; -.
DR   EMDB; EMD-8133; -.
DR   EMDB; EMD-8134; -.
DR   EMDB; EMD-8135; -.
DR   EMDB; EMD-8136; -.
DR   EMDB; EMD-8137; -.
DR   EMDB; EMD-8138; -.
DR   EMDB; EMD-9306; -.
DR   SMR; P52655; -.
DR   BioGRID; 109212; 82.
DR   ComplexPortal; CPX-519; General transcription factor complex TFIIA.
DR   CORUM; P52655; -.
DR   DIP; DIP-33225N; -.
DR   IntAct; P52655; 27.
DR   MINT; P52655; -.
DR   STRING; 9606.ENSP00000452454; -.
DR   BindingDB; P52655; -.
DR   ChEMBL; CHEMBL4832; -.
DR   GlyCosmos; P52655; 7 sites, 2 glycans.
DR   GlyGen; P52655; 7 sites, 2 O-linked glycans (7 sites).
DR   iPTMnet; P52655; -.
DR   PhosphoSitePlus; P52655; -.
DR   BioMuta; GTF2A1; -.
DR   DMDM; 1711663; -.
DR   EPD; P52655; -.
DR   jPOST; P52655; -.
DR   MassIVE; P52655; -.
DR   MaxQB; P52655; -.
DR   PaxDb; 9606-ENSP00000452454; -.
DR   PeptideAtlas; P52655; -.
DR   ProteomicsDB; 56499; -. [P52655-1]
DR   ProteomicsDB; 56500; -. [P52655-2]
DR   Pumba; P52655; -.
DR   Antibodypedia; 76; 347 antibodies from 32 providers.
DR   DNASU; 2957; -.
DR   Ensembl; ENST00000434192.2; ENSP00000409492.2; ENSG00000165417.12. [P52655-2]
DR   Ensembl; ENST00000553612.6; ENSP00000452454.1; ENSG00000165417.12. [P52655-1]
DR   GeneID; 2957; -.
DR   KEGG; hsa:2957; -.
DR   MANE-Select; ENST00000553612.6; ENSP00000452454.1; NM_015859.4; NP_056943.1.
DR   UCSC; uc001xvf.4; human. [P52655-1]
DR   AGR; HGNC:4646; -.
DR   CTD; 2957; -.
DR   DisGeNET; 2957; -.
DR   GeneCards; GTF2A1; -.
DR   HGNC; HGNC:4646; GTF2A1.
DR   HPA; ENSG00000165417; Low tissue specificity.
DR   MIM; 600520; gene.
DR   neXtProt; NX_P52655; -.
DR   OpenTargets; ENSG00000165417; -.
DR   PharmGKB; PA29033; -.
DR   VEuPathDB; HostDB:ENSG00000165417; -.
DR   eggNOG; KOG2652; Eukaryota.
DR   GeneTree; ENSGT00940000156726; -.
DR   HOGENOM; CLU_030027_5_0_1; -.
DR   InParanoid; P52655; -.
DR   OMA; EVCDASQ; -.
DR   OrthoDB; 9955at2759; -.
DR   PhylomeDB; P52655; -.
DR   TreeFam; TF350445; -.
DR   PathwayCommons; P52655; -.
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; P52655; -.
DR   SIGNOR; P52655; -.
DR   BioGRID-ORCS; 2957; 660 hits in 1169 CRISPR screens.
DR   ChiTaRS; GTF2A1; human.
DR   EvolutionaryTrace; P52655; -.
DR   GeneWiki; GTF2A1; -.
DR   GenomeRNAi; 2957; -.
DR   Pharos; P52655; Tchem.
DR   PRO; PR:P52655; -.
DR   Proteomes; UP000005640; Chromosome 14.
DR   RNAct; P52655; Protein.
DR   Bgee; ENSG00000165417; Expressed in esophagus squamous epithelium and 192 other cell types or tissues.
DR   ExpressionAtlas; P52655; baseline and differential.
DR   GO; GO:0005829; C:cytosol; 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:0097550; C:transcription preinitiation complex; IDA:GO_Central.
DR   GO; GO:0003677; F:DNA binding; IDA:BHF-UCL.
DR   GO; GO:0046982; F:protein heterodimerization activity; IPI:BHF-UCL.
DR   GO; GO:0000979; F:RNA polymerase II core promoter sequence-specific DNA binding; IDA:ARUK-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:ARUK-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 by RNA polymerase II; IDA:ComplexPortal.
DR   GO; GO:0051123; P:RNA polymerase II preinitiation complex assembly; NAS:ComplexPortal.
DR   GO; GO:0006366; P:transcription by RNA polymerase II; IDA:ARUK-UCL.
DR   CDD; cd07976; TFIIA_alpha_beta_like; 2.
DR   Gene3D; 1.10.287.100; -; 1.
DR   Gene3D; 2.30.18.10; Transcription factor IIA (TFIIA), beta-barrel domain; 1.
DR   IDEAL; IID00555; -.
DR   InterPro; IPR004855; TFIIA_asu/bsu.
DR   InterPro; IPR009088; TFIIA_b-brl.
DR   PANTHER; PTHR12694; TRANSCRIPTION INITIATION FACTOR IIA SUBUNIT 1; 1.
DR   PANTHER; PTHR12694:SF7; TRANSCRIPTION INITIATION FACTOR IIA SUBUNIT 1; 1.
DR   Pfam; PF03153; TFIIA; 2.
DR   SMART; SM01371; TFIIA; 1.
DR   SUPFAM; SSF47396; Transcription factor IIA (TFIIA), alpha-helical domain; 1.
DR   SUPFAM; SSF50784; Transcription factor IIA (TFIIA), beta-barrel domain; 1.
DR   Genevisible; P52655; HS.
PE   1: Evidence at protein level;
KW   3D-structure; Acetylation; Alternative initiation;
KW   Direct protein sequencing; Nucleus; Phosphoprotein; Reference proteome;
KW   Transcription; Transcription regulation.
FT   INIT_MET        1
FT                   /note="Removed"
FT                   /evidence="ECO:0007744|PubMed:19413330,
FT                   ECO:0007744|PubMed:22814378"
FT   CHAIN           2..376
FT                   /note="Transcription initiation factor IIA subunit 1"
FT                   /id="PRO_0000022481"
FT   CHAIN           2..274
FT                   /note="Transcription initiation factor IIA alpha chain"
FT                   /id="PRO_0000042593"
FT   CHAIN           275..376
FT                   /note="Transcription initiation factor IIA beta chain"
FT                   /id="PRO_0000042594"
FT   REGION          69..107
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          247..266
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          274..329
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        90..107
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        278..329
FT                   /note="Acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         343
FT                   /ligand="DNA"
FT                   /ligand_id="ChEBI:CHEBI:16991"
FT                   /evidence="ECO:0000269|PubMed:27193682,
FT                   ECO:0007744|PDB:5IYD"
FT   BINDING         344
FT                   /ligand="DNA"
FT                   /ligand_id="ChEBI:CHEBI:16991"
FT                   /evidence="ECO:0000269|PubMed:27193682,
FT                   ECO:0007744|PDB:5IYD"
FT   SITE            274..275
FT                   /note="Cleavage; by TASP1"
FT   MOD_RES         2
FT                   /note="N-acetylalanine"
FT                   /evidence="ECO:0007744|PubMed:19413330,
FT                   ECO:0007744|PubMed:22814378"
FT   MOD_RES         280
FT                   /note="Phosphoserine; by TAF1"
FT                   /evidence="ECO:0000269|PubMed:11278496"
FT   MOD_RES         281
FT                   /note="Phosphoserine; by TAF1"
FT                   /evidence="ECO:0000269|PubMed:11278496"
FT   MOD_RES         316
FT                   /note="Phosphoserine; by TAF1"
FT                   /evidence="ECO:0000269|PubMed:11278496,
FT                   ECO:0007744|PubMed:17081983"
FT   MOD_RES         321
FT                   /note="Phosphoserine; by TAF1"
FT                   /evidence="ECO:0000269|PubMed:11278496,
FT                   ECO:0007744|PubMed:17081983"
FT   VAR_SEQ         1..39
FT                   /note="Missing (in isoform 37 kDa)"
FT                   /evidence="ECO:0000305"
FT                   /id="VSP_018798"
FT   VARIANT         30
FT                   /note="L -> V (in a breast cancer sample; somatic
FT                   mutation)"
FT                   /evidence="ECO:0000269|PubMed:16959974"
FT                   /id="VAR_035667"
FT   VARIANT         109
FT                   /note="A -> P (in dbSNP:rs17111579)"
FT                   /id="VAR_054043"
FT   MUTAGEN         270
FT                   /note="V->A: Slightly affects cleavage and yields elevated
FT                   levels of the precursor."
FT                   /evidence="ECO:0000269|PubMed:15257296"
FT   MUTAGEN         272
FT                   /note="Q->A: Abolishes cleavage."
FT                   /evidence="ECO:0000269|PubMed:15257296"
FT   MUTAGEN         273
FT                   /note="V->A: Abolishes cleavage."
FT                   /evidence="ECO:0000269|PubMed:15257296"
FT   MUTAGEN         274
FT                   /note="D->A: Abolishes cleavage."
FT                   /evidence="ECO:0000269|PubMed:15257296"
FT   MUTAGEN         275
FT                   /note="G->A: Abolishes cleavage."
FT                   /evidence="ECO:0000269|PubMed:15257296"
FT   MUTAGEN         276
FT                   /note="T->A: Does not affect cleavage."
FT                   /evidence="ECO:0000269|PubMed:15257296"
FT   MUTAGEN         277
FT                   /note="G->A: Does not affect cleavage."
FT                   /evidence="ECO:0000269|PubMed:15257296"
FT   MUTAGEN         278
FT                   /note="D->A: Significant reduction of cleavage."
FT                   /evidence="ECO:0000269|PubMed:15257296"
FT   MUTAGEN         280
FT                   /note="S->A: Slightly affects cleavage, yields elevated
FT                   levels of the precursor. Eliminates phosphorylation; when
FT                   associated with A-281; A-316 and A-321."
FT                   /evidence="ECO:0000269|PubMed:11278496,
FT                   ECO:0000269|PubMed:15257296"
FT   MUTAGEN         281
FT                   /note="S->A: Eliminates phosphorylation; when associated
FT                   with A-280; A-316 and A-321."
FT                   /evidence="ECO:0000269|PubMed:11278496"
FT   MUTAGEN         282
FT                   /note="E->A: Slightly affects cleavage and yields elevated
FT                   levels of the precursor."
FT                   /evidence="ECO:0000269|PubMed:15257296"
FT   MUTAGEN         316
FT                   /note="S->A: Strongly reduces phosphorylation; when
FT                   associated with A-321. Eliminates phosphorylation; when
FT                   associated with A-280; A-281 and A-321."
FT                   /evidence="ECO:0000269|PubMed:11278496"
FT   MUTAGEN         321
FT                   /note="S->A: Strongly reduces phosphorylation; when
FT                   associated with A-316. Eliminates phosphorylation; when
FT                   associated with A-280; A-281 and A-316."
FT                   /evidence="ECO:0000269|PubMed:11278496"
FT   HELIX           10..32
FT                   /evidence="ECO:0007829|PDB:1NVP"
FT   HELIX           36..50
FT                   /evidence="ECO:0007829|PDB:1NVP"
FT   STRAND          65..76
FT                   /evidence="ECO:0007829|PDB:5M4S"
FT   STRAND          79..83
FT                   /evidence="ECO:0007829|PDB:5M4S"
FT   HELIX           325..329
FT                   /evidence="ECO:0007829|PDB:7NVU"
FT   STRAND          334..345
FT                   /evidence="ECO:0007829|PDB:1NVP"
FT   STRAND          348..360
FT                   /evidence="ECO:0007829|PDB:1NVP"
FT   STRAND          363..375
FT                   /evidence="ECO:0007829|PDB:1NVP"
SQ   SEQUENCE   376 AA;  41514 MW;  4BAE1853E7E89218 CRC64;
     MANSANTNTV PKLYRSVIED VINDVRDIFL DDGVDEQVLM ELKTLWENKL MQSRAVDGFH
     SEEQQLLLQV QQQHQPQQQQ HHHHHHHQQA QPQQTVPQQA QTQQVLIPAS QQATAPQVIV
     PDSKLIQHMN ASNMSAAATA ATLALPAGVT PVQQILTNSG QLLQVVRAAN GAQYIFQPQQ
     SVVLQQQVIP QMQPGGVQAP VIQQVLAPLP GGISPQTGVI IQPQQILFTG NKTQVIPTTV
     AAPTPAQAQI TATGQQQPQA QPAQTQAPLV LQVDGTGDTS SEEDEDEEED YDDDEEEDKE
     KDGAEDGQVE EEPLNSEDDV SDEEGQELFD TENVVVCQYD KIHRSKNKWK FHLKDGIMNL
     NGRDYIFSKA IGDAEW
//