TF2AA_HUMAN
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 03-AUG-2022, entry version 209.
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 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. {ECO:0000269|PubMed:11030333}.
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 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 AlphaFoldDB; P52655; -.
DR SMR; P52655; -.
DR BioGRID; 109212; 76.
DR ComplexPortal; CPX-519; Transcription factor complex TFIIA.
DR CORUM; P52655; -.
DR DIP; DIP-33225N; -.
DR IntAct; P52655; 26.
DR MINT; P52655; -.
DR STRING; 9606.ENSP00000452454; -.
DR BindingDB; P52655; -.
DR ChEMBL; CHEMBL4832; -.
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; P52655; -.
DR PeptideAtlas; P52655; -.
DR PRIDE; P52655; -.
DR ProteomicsDB; 56499; -. [P52655-1]
DR ProteomicsDB; 56500; -. [P52655-2]
DR Antibodypedia; 76; 313 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 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; 1443035at2759; -.
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; 633 hits in 1091 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 190 other tissues.
DR ExpressionAtlas; P52655; baseline and differential.
DR Genevisible; P52655; HS.
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 from RNA polymerase II promoter; IDA:ComplexPortal.
DR GO; GO:0051123; P:RNA polymerase II preinitiation complex assembly; IC:ComplexPortal.
DR GO; GO:0006366; P:transcription by RNA polymerase II; IDA:ARUK-UCL.
DR Gene3D; 2.30.18.10; -; 1.
DR IDEAL; IID00555; -.
DR InterPro; IPR004855; TFIIA_asu/bsu.
DR InterPro; IPR009088; TFIIA_b-brl.
DR PANTHER; PTHR12694; PTHR12694; 1.
DR Pfam; PF03153; TFIIA; 2.
DR SMART; SM01371; TFIIA; 1.
DR SUPFAM; SSF50784; SSF50784; 1.
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 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
