BRF2_HUMAN
ID BRF2_HUMAN Reviewed; 419 AA.
AC Q9HAW0; B2RD62; B4DFZ6; D3DSW6; Q9H2Y3; Q9H3B3; Q9NUY6;
DT 20-MAY-2008, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2001, sequence version 1.
DT 03-AUG-2022, entry version 175.
DE RecName: Full=Transcription factor IIIB 50 kDa subunit;
DE Short=TFIIIB50 {ECO:0000303|PubMed:11121026};
DE Short=hTFIIIB50 {ECO:0000303|PubMed:11121026};
DE AltName: Full=B-related factor 2;
DE Short=BRF-2;
DE AltName: Full=hBRFU;
GN Name=BRF2; Synonyms=BRFU {ECO:0000303|PubMed:11040218}; ORFNames=PRO1470;
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] (ISOFORM 1), AND FUNCTION.
RX PubMed=11040218; DOI=10.1101/gad.836400;
RA Schramm L., Pendergrast P.S., Sun Y., Hernandez N.;
RT "Different human TFIIIB activities direct RNA polymerase III transcription
RT from TATA-containing and TATA-less promoters.";
RL Genes Dev. 14:2650-2663(2000).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), AND FUNCTION.
RX PubMed=11121026; DOI=10.1073/pnas.97.26.14200;
RA Teichmann M., Wang Z., Roeder R.G.;
RT "A stable complex of a novel transcription factor IIB- related factor,
RT human TFIIIB50, and associated proteins mediate selective transcription by
RT RNA polymerase III of genes with upstream promoter elements.";
RL Proc. Natl. Acad. Sci. U.S.A. 97:14200-14205(2000).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
RC TISSUE=Amygdala, Placenta, and Umbilical cord blood;
RX PubMed=14702039; DOI=10.1038/ng1285;
RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H.,
RA Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M.,
RA Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K.,
RA Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T.,
RA Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M.,
RA Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S.,
RA Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H.,
RA Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K.,
RA Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N.,
RA Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y.,
RA Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K.,
RA Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T.,
RA Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T.,
RA Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y.,
RA Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H.,
RA Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y.,
RA Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H.,
RA Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O.,
RA Isogai T., Sugano S.;
RT "Complete sequencing and characterization of 21,243 full-length human
RT cDNAs.";
RL Nat. Genet. 36:40-45(2004).
RN [4]
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 (SEP-2005) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Eye;
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 NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 264-419 (ISOFORM 1).
RC TISSUE=Fetal liver;
RX PubMed=11483580; DOI=10.1101/gr.175501;
RA Yu Y., Zhang C., Zhou G., Wu S., Qu X., Wei H., Xing G., Dong C., Zhai Y.,
RA Wan J., Ouyang S., Li L., Zhang S., Zhou K., Zhang Y., Wu C., He F.;
RT "Gene expression profiling in human fetal liver and identification of
RT tissue- and developmental-stage-specific genes through compiled expression
RT profiles and efficient cloning of full-length cDNAs.";
RL Genome Res. 11:1392-1403(2001).
RN [7]
RP FUNCTION, AND INTERACTION WITH TBP.
RX PubMed=11564744; DOI=10.1074/jbc.m108515200;
RA Cabart P., Murphy S.;
RT "BRFU, a TFIIB-like factor, is directly recruited to the TATA-box of
RT polymerase III small nuclear RNA gene promoters through its interaction
RT with TATA-binding protein.";
RL J. Biol. Chem. 276:43056-43064(2001).
RN [8]
RP IDENTIFICATION IN THE TFIIIB-ALPHA COMPLEX.
RX PubMed=12016223; DOI=10.1074/jbc.m203119200;
RA Cabart P., Murphy S.;
RT "Assembly of human small nuclear RNA gene-specific transcription factor
RT IIIB complex de novo on and off promoter.";
RL J. Biol. Chem. 277:26831-26838(2002).
RN [9]
RP SUBUNIT.
RX PubMed=12391172; DOI=10.1128/mcb.22.22.8067-8078.2002;
RA Ma B., Hernandez N.;
RT "Redundant cooperative interactions for assembly of a human U6
RT transcription initiation complex.";
RL Mol. Cell. Biol. 22:8067-8078(2002).
RN [10]
RP INTERACTION WITH SNAPC4, AND SUBUNIT.
RX PubMed=12621023; DOI=10.1074/jbc.m204247200;
RA Hinkley C.S., Hirsch H.A., Gu L., LaMere B., Henry R.W.;
RT "The small nuclear RNA-activating protein 190 Myb DNA binding domain
RT stimulates TATA box-binding protein-TATA box recognition.";
RL J. Biol. Chem. 278:18649-18657(2003).
RN [11]
RP SUBUNIT.
RX PubMed=14527415; DOI=10.1016/j.molcel.2003.08.011;
RA Hu P., Wu S., Hernandez N.;
RT "A minimal RNA polymerase III transcription system from human cells reveals
RT positive and negative regulatory roles for CK2.";
RL Mol. Cell 12:699-709(2003).
RN [12]
RP SUBUNIT.
RX PubMed=16227591; DOI=10.1128/mcb.25.21.9406-9418.2005;
RA Saxena A., Ma B., Schramm L., Hernandez N.;
RT "Structure-function analysis of the human TFIIB-related factor II protein
RT reveals an essential role for the C-terminal domain in RNA polymerase III
RT transcription.";
RL Mol. Cell. Biol. 25:9406-9418(2005).
RN [13]
RP SUBUNIT.
RX PubMed=16769183; DOI=10.1016/j.gene.2006.03.012;
RA Emran F., Florens L., Ma B., Swanson S.K., Washburn M.P., Hernandez N.;
RT "A role for Yin Yang-1 (YY1) in the assembly of snRNA transcription
RT complexes.";
RL Gene 377:96-108(2006).
RN [14]
RP INTERACTION WITH MAF1, AND SUBCELLULAR LOCATION.
RX PubMed=17505538; DOI=10.7150/ijbs.3.292;
RA Rollins J., Veras I., Cabarcas S., Willis I., Schramm L.;
RT "Human Maf1 negatively regulates RNA polymerase III transcription via the
RT TFIIB family members Brf1 and Brf2.";
RL Int. J. Biol. Sci. 3:292-302(2007).
RN [15]
RP INDUCTION.
RX PubMed=17624304; DOI=10.1016/j.bbrc.2007.06.114;
RA Jacob J., Cabarcas S., Veras I., Zaveri N., Schramm L.;
RT "The green tea component EGCG inhibits RNA polymerase III transcription.";
RL Biochem. Biophys. Res. Commun. 360:778-783(2007).
RN [16]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=18669648; DOI=10.1073/pnas.0805139105;
RA Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,
RA Elledge S.J., Gygi S.P.;
RT "A quantitative atlas of mitotic phosphorylation.";
RL Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
RN [17]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-353, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Erythroleukemia;
RX PubMed=23186163; DOI=10.1021/pr300630k;
RA Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J.,
RA Mohammed S.;
RT "Toward a comprehensive characterization of a human cancer cell
RT phosphoproteome.";
RL J. Proteome Res. 12:260-271(2013).
RN [18] {ECO:0007744|PDB:4ROC, ECO:0007744|PDB:4ROD, ECO:0007744|PDB:4ROE}
RP X-RAY CRYSTALLOGRAPHY (1.90 ANGSTROMS) OF 62-419 IN COMPLEX WITH TBP AND
RP DNA, FUNCTION, INTERACTION WITH TBP, SUBUNIT, DNA-BINDING, MUTAGENESIS OF
RP ARG-110 AND CYS-361, OXIDATION AT CYS-361, AND IDENTIFICATION BY MASS
RP SPECTROMETRY.
RX PubMed=26638071; DOI=10.1016/j.cell.2015.11.005;
RA Gouge J., Satia K., Guthertz N., Widya M., Thompson A.J., Cousin P.,
RA Dergai O., Hernandez N., Vannini A.;
RT "Redox signaling by the RNA polymerase III TFIIB-related factor Brf2.";
RL Cell 163:1375-1387(2015).
CC -!- FUNCTION: General activator of RNA polymerase III transcription. Factor
CC exclusively required for RNA polymerase III transcription of genes with
CC promoter elements upstream of the initiation sites (PubMed:11040218,
CC PubMed:11121026, PubMed:11564744, PubMed:26638071). Contributes to the
CC regulation of gene expression; functions as activator in the absence of
CC oxidative stress (PubMed:26638071). Down-regulates expression of target
CC genes in response to oxidative stress (PubMed:26638071). Overexpression
CC protects cells against apoptosis in response to oxidative stress
CC (PubMed:26638071). {ECO:0000269|PubMed:11040218,
CC ECO:0000269|PubMed:11121026, ECO:0000269|PubMed:11564744,
CC ECO:0000269|PubMed:26638071}.
CC -!- SUBUNIT: Component of TFIIIB complexes. The TFIIIB complex has two
CC activities, alpha and beta. The TFIIIB-alpha activity complex is
CC composed of TBP, BDP1, and a complex containing both BRF2 and at least
CC four stably associated proteins; this complex inhibits the
CC transcription by pol III via its phosphorylation by CK2; YY1
CC facilitates the TFIIIB-alpha complex formation. Interacts with TBP;
CC this interaction promotes recruitment of BRF2 to TATA box-containing
CC promoters (PubMed:26638071). Interacts with TBP and the BURE sequence
CC (GC-rich sequence downstream from the TATA box) to form a strong
CC ternary complex which is joined by BDP1; this ternary complex
CC stimulates pol III transcription. Forms a trimeric complex composed of
CC TBP, BRF2 and mini-SNAPc complex (SNAP43, SNAP50, and the N-terminal
CC third of SNAP190) on the promoter. Assembly of the TBP-BRF2 complex is
CC stimulated by SNAP190. Interacts with MAF1 and SNAPC4.
CC {ECO:0000269|PubMed:11564744, ECO:0000269|PubMed:12016223,
CC ECO:0000269|PubMed:12391172, ECO:0000269|PubMed:12621023,
CC ECO:0000269|PubMed:14527415, ECO:0000269|PubMed:16227591,
CC ECO:0000269|PubMed:16769183, ECO:0000269|PubMed:17505538,
CC ECO:0000269|PubMed:26638071}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:17505538}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q9HAW0-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q9HAW0-2; Sequence=VSP_056834;
CC -!- INDUCTION: Down-regulated by epigallocatechin gallate (EGCG) treatment.
CC {ECO:0000269|PubMed:17624304}.
CC -!- PTM: In response to oxidative stress, Cys-361 is reversibly oxidized to
CC cysteine sulfenic acid. Oxidation of Cys-361 impairs formation of a
CC ternary complex with TBP and DNA and down-regulates expression of
CC target genes in response to oxidative stress.
CC {ECO:0000269|PubMed:26638071}.
CC -!- SIMILARITY: Belongs to the TFIIB family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAG35486.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; AF298153; AAG30222.1; -; mRNA.
DR EMBL; AF206673; AAG35669.2; -; mRNA.
DR EMBL; AK001914; BAA91975.1; -; mRNA.
DR EMBL; AK294337; BAG57607.1; -; mRNA.
DR EMBL; AK315420; BAG37809.1; -; mRNA.
DR EMBL; CH471080; EAW63351.1; -; Genomic_DNA.
DR EMBL; CH471080; EAW63352.1; -; Genomic_DNA.
DR EMBL; CH471080; EAW63353.1; -; Genomic_DNA.
DR EMBL; BC010648; AAH10648.1; -; mRNA.
DR EMBL; AF130058; AAG35486.1; ALT_INIT; mRNA.
DR CCDS; CCDS6098.1; -. [Q9HAW0-1]
DR RefSeq; NP_060780.2; NM_018310.3. [Q9HAW0-1]
DR PDB; 4ROC; X-ray; 1.90 A; A=62-419.
DR PDB; 4ROD; X-ray; 2.70 A; A=62-419.
DR PDB; 4ROE; X-ray; 2.20 A; A=62-419.
DR PDB; 5N9G; X-ray; 2.70 A; A/F=62-419.
DR PDBsum; 4ROC; -.
DR PDBsum; 4ROD; -.
DR PDBsum; 4ROE; -.
DR PDBsum; 5N9G; -.
DR AlphaFoldDB; Q9HAW0; -.
DR SMR; Q9HAW0; -.
DR BioGRID; 120578; 37.
DR IntAct; Q9HAW0; 3.
DR STRING; 9606.ENSP00000220659; -.
DR iPTMnet; Q9HAW0; -.
DR PhosphoSitePlus; Q9HAW0; -.
DR BioMuta; BRF2; -.
DR DMDM; 74734246; -.
DR EPD; Q9HAW0; -.
DR jPOST; Q9HAW0; -.
DR MassIVE; Q9HAW0; -.
DR MaxQB; Q9HAW0; -.
DR PaxDb; Q9HAW0; -.
DR PeptideAtlas; Q9HAW0; -.
DR PRIDE; Q9HAW0; -.
DR ProteomicsDB; 81450; -. [Q9HAW0-1]
DR Antibodypedia; 10831; 132 antibodies from 27 providers.
DR DNASU; 55290; -.
DR Ensembl; ENST00000220659.11; ENSP00000220659.6; ENSG00000104221.13. [Q9HAW0-1]
DR GeneID; 55290; -.
DR KEGG; hsa:55290; -.
DR MANE-Select; ENST00000220659.11; ENSP00000220659.6; NM_018310.4; NP_060780.2.
DR UCSC; uc003xkk.4; human. [Q9HAW0-1]
DR CTD; 55290; -.
DR DisGeNET; 55290; -.
DR GeneCards; BRF2; -.
DR HGNC; HGNC:17298; BRF2.
DR HPA; ENSG00000104221; Low tissue specificity.
DR MIM; 607013; gene.
DR neXtProt; NX_Q9HAW0; -.
DR OpenTargets; ENSG00000104221; -.
DR PharmGKB; PA164741329; -.
DR VEuPathDB; HostDB:ENSG00000104221; -.
DR eggNOG; KOG1598; Eukaryota.
DR GeneTree; ENSGT00390000002288; -.
DR HOGENOM; CLU_039947_0_0_1; -.
DR InParanoid; Q9HAW0; -.
DR OMA; LARFCKM; -.
DR OrthoDB; 1518547at2759; -.
DR PhylomeDB; Q9HAW0; -.
DR TreeFam; TF331596; -.
DR PathwayCommons; Q9HAW0; -.
DR Reactome; R-HSA-749476; RNA Polymerase III Abortive And Retractive Initiation.
DR Reactome; R-HSA-76071; RNA Polymerase III Transcription Initiation From Type 3 Promoter.
DR SignaLink; Q9HAW0; -.
DR SIGNOR; Q9HAW0; -.
DR BioGRID-ORCS; 55290; 788 hits in 1085 CRISPR screens.
DR ChiTaRS; BRF2; human.
DR GeneWiki; BRF2_(gene); -.
DR GenomeRNAi; 55290; -.
DR Pharos; Q9HAW0; Tbio.
DR PRO; PR:Q9HAW0; -.
DR Proteomes; UP000005640; Chromosome 8.
DR RNAct; Q9HAW0; protein.
DR Bgee; ENSG00000104221; Expressed in skeletal muscle tissue of rectus abdominis and 204 other tissues.
DR ExpressionAtlas; Q9HAW0; baseline and differential.
DR Genevisible; Q9HAW0; HS.
DR GO; GO:0005654; C:nucleoplasm; TAS:Reactome.
DR GO; GO:0005634; C:nucleus; IBA:GO_Central.
DR GO; GO:0000126; C:transcription factor TFIIIB complex; IMP:UniProtKB.
DR GO; GO:0097550; C:transcription preinitiation complex; IBA:GO_Central.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0001006; F:RNA polymerase III type 3 promoter sequence-specific DNA binding; IDA:UniProtKB.
DR GO; GO:0017025; F:TBP-class protein binding; IBA:GO_Central.
DR GO; GO:0034599; P:cellular response to oxidative stress; IMP:UniProtKB.
DR GO; GO:0006352; P:DNA-templated transcription, initiation; IBA:GO_Central.
DR GO; GO:0006359; P:regulation of transcription by RNA polymerase III; IMP:UniProtKB.
DR GO; GO:0070897; P:transcription preinitiation complex assembly; IEA:InterPro.
DR InterPro; IPR036915; Cyclin-like_sf.
DR InterPro; IPR000812; TFIIB.
DR InterPro; IPR013137; Znf_TFIIB.
DR PANTHER; PTHR11618; PTHR11618; 1.
DR Pfam; PF08271; TF_Zn_Ribbon; 1.
DR SUPFAM; SSF47954; SSF47954; 1.
DR PROSITE; PS51134; ZF_TFIIB; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Activator; Alternative splicing; Metal-binding; Nucleus;
KW Oxidation; Phosphoprotein; Reference proteome; Repeat; Stress response;
KW Transcription; Transcription regulation; Zinc; Zinc-finger.
FT CHAIN 1..419
FT /note="Transcription factor IIIB 50 kDa subunit"
FT /id="PRO_0000337187"
FT REPEAT 72..157
FT /note="1"
FT REPEAT 173..249
FT /note="2"
FT ZN_FING 2..36
FT /note="TFIIB-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00469"
FT REGION 108..114
FT /note="Interaction with target DNA"
FT /evidence="ECO:0000269|PubMed:26638071,
FT ECO:0007744|PDB:4ROC, ECO:0007744|PDB:4ROD,
FT ECO:0007744|PDB:4ROE"
FT REGION 314..351
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 357..363
FT /note="Required for the formation of a ternary complex with
FT DNA and TBP; not required for interaction with TBP in the
FT absence of DNA"
FT /evidence="ECO:0000269|PubMed:26638071"
FT REGION 365..419
FT /note="Required for interaction with TBP and formation of a
FT ternary complex with DNA and TBP"
FT /evidence="ECO:0000269|PubMed:26638071"
FT BINDING 7
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00469"
FT BINDING 10
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00469"
FT BINDING 28
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00469"
FT BINDING 31
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00469"
FT MOD_RES 353
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 361
FT /note="Cysteine sulfenic acid (-SOH)"
FT /evidence="ECO:0000269|PubMed:26638071"
FT VAR_SEQ 10..32
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_056834"
FT MUTAGEN 110
FT /note="R->A: Decreases affinity for DNA."
FT /evidence="ECO:0000269|PubMed:26638071"
FT MUTAGEN 361
FT /note="C->A: Abolishes response to oxidative stress.
FT Abolishes the decrease in the formation of a ternary
FT complex with DNA and TBP in response to oxidative stress."
FT /evidence="ECO:0000269|PubMed:26638071"
FT MUTAGEN 361
FT /note="C->D: Impairs formation of a ternary complex with
FT DNA and TBP."
FT /evidence="ECO:0000269|PubMed:26638071"
FT CONFLICT 153
FT /note="Y -> C (in Ref. 3; BAA91975)"
FT /evidence="ECO:0000305"
FT CONFLICT 376
FT /note="S -> F (in Ref. 2; AAG35669)"
FT /evidence="ECO:0000305"
FT CONFLICT 379
FT /note="T -> I (in Ref. 3; BAG57607)"
FT /evidence="ECO:0000305"
FT HELIX 67..82
FT /evidence="ECO:0007829|PDB:4ROC"
FT HELIX 87..101
FT /evidence="ECO:0007829|PDB:4ROC"
FT HELIX 104..107
FT /evidence="ECO:0007829|PDB:4ROC"
FT HELIX 111..128
FT /evidence="ECO:0007829|PDB:4ROC"
FT HELIX 135..142
FT /evidence="ECO:0007829|PDB:4ROC"
FT HELIX 146..159
FT /evidence="ECO:0007829|PDB:4ROC"
FT HELIX 169..178
FT /evidence="ECO:0007829|PDB:4ROC"
FT HELIX 191..193
FT /evidence="ECO:0007829|PDB:4ROC"
FT HELIX 197..213
FT /evidence="ECO:0007829|PDB:4ROC"
FT HELIX 223..237
FT /evidence="ECO:0007829|PDB:4ROC"
FT HELIX 239..242
FT /evidence="ECO:0007829|PDB:4ROC"
FT HELIX 247..253
FT /evidence="ECO:0007829|PDB:4ROC"
FT HELIX 262..277
FT /evidence="ECO:0007829|PDB:4ROC"
FT HELIX 281..284
FT /evidence="ECO:0007829|PDB:4ROC"
FT TURN 285..287
FT /evidence="ECO:0007829|PDB:4ROE"
FT TURN 290..293
FT /evidence="ECO:0007829|PDB:4ROC"
FT HELIX 294..296
FT /evidence="ECO:0007829|PDB:4ROC"
FT HELIX 297..302
FT /evidence="ECO:0007829|PDB:4ROC"
FT HELIX 304..313
FT /evidence="ECO:0007829|PDB:4ROC"
FT TURN 360..362
FT /evidence="ECO:0007829|PDB:4ROC"
FT HELIX 386..390
FT /evidence="ECO:0007829|PDB:4ROC"
FT HELIX 396..406
FT /evidence="ECO:0007829|PDB:4ROC"
SQ SEQUENCE 419 AA; 46533 MW; 90A39F72DBA14888 CRC64;
MPGRGRCPDC GSTELVEDSH YSQSQLVCSD CGCVVTEGVL TTTFSDEGNL REVTYSRSTG
ENEQVSRSQQ RGLRRVRDLC RVLQLPPTFE DTAVAYYQQA YRHSGIRAAR LQKKEVLVGC
CVLITCRQHN WPLTMGAICT LLYADLDVFS STYMQIVKLL GLDVPSLCLA ELVKTYCSSF
KLFQASPSVP AKYVEDKEKM LSRTMQLVEL ANETWLVTGR HPLPVITAAT FLAWQSLQPA
DRLSCSLARF CKLANVDLPY PASSRLQELL AVLLRMAEQL AWLRVLRLDK RSVVKHIGDL
LQHRQSLVRS AFRDGTAEVE TREKEPPGWG QGQGEGEVGN NSLGLPQGKR PASPALLLPP
CMLKSPKRIC PVPPVSTVTG DENISDSEIE QYLRTPQEVR DFQRAQAARQ AATSVPNPP
