ID T2EA_HUMAN Reviewed; 439 AA. AC P29083; Q16103; DT 01-DEC-1992, integrated into UniProtKB/Swiss-Prot. DT 17-OCT-2006, sequence version 2. DT 02-SEP-2026, entry version 223. DE RecName: Full=General transcription factor IIE subunit 1; DE AltName: Full=General transcription factor IIE 56 kDa subunit; DE AltName: Full=Transcription initiation factor IIE subunit alpha; DE Short=TFIIE-alpha; GN Name=GTF2E1; Synonyms=TF2E1; 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], PARTIAL PROTEIN SEQUENCE, SUBUNIT, AND RP SUBCELLULAR LOCATION. RX PubMed=1956398; DOI=10.1038/354369a0; RA Peterson M.G., Inostroza J., Maxon M.E., Flores O., Admon A., Reinberg D., RA Tjian R.; RT "Structure and functional properties of human general transcription factor RT IIE."; RL Nature 354:369-373(1991). RN [2] RP NUCLEOTIDE SEQUENCE [MRNA], AND PARTIAL PROTEIN SEQUENCE. RX PubMed=1956403; DOI=10.1038/354398a0; RA Ohkuma Y., Sumimoto H., Hoffmann A., Shimasaki S., Horikoshi M., RA Roeder R.G.; RT "Structural motifs and potential sigma homologies in the large subunit of RT human general transcription factor TFIIE."; RL Nature 354:398-401(1991). RN [3] RP PROTEIN SEQUENCE OF 2-16; 154-170; 219-236; 243-266 AND 402-423, CLEAVAGE RP OF INITIATOR METHIONINE, ACETYLATION AT ALA-2, AND IDENTIFICATION BY MASS RP SPECTROMETRY. RC TISSUE=Ovarian carcinoma; RA Bienvenut W.V.; RL Submitted (JAN-2010) to UniProtKB. RN [4] RP INTERACTION WITH SND1, AND SUBCELLULAR LOCATION. RX PubMed=7651391; DOI=10.1128/mcb.15.9.4735; RA Tong X., Drapkin R., Yalamanchili R., Mosialos G., Kieff E.; RT "The Epstein-Barr virus nuclear protein 2 acidic domain forms a complex RT with a novel cellular coactivator that can interact with TFIIE."; RL Mol. Cell. Biol. 15:4735-4744(1995). RN [5] RP INTERACTION WITH TAF6. RX PubMed=7667268; DOI=10.1073/pnas.92.18.8195; RA Hisatake K., Ohta T., Takada R., Guermah M., Horikoshi M., Nakatani Y., RA Roeder R.G.; RT "Evolutionary conservation of human TATA-binding-polypeptide-associated RT factors TAFII31 and TAFII80 and interactions of TAFII80 with other TAFs and RT with general transcription factors."; RL Proc. Natl. Acad. Sci. U.S.A. 92:8195-8199(1995). RN [6] RP INTERACTION WITH VARICELLA-ZOSTER VIRUS IE63 PROTEIN (MICROBIAL INFECTION). RX PubMed=15843171; DOI=10.1515/bc.2005.031; RA Di Valentin E., Bontems S., Habran L., Jolois O., Markine-Goriaynoff N., RA Vanderplasschen A., Sadzot-Delvaux C., Piette J.; RT "Varicella-zoster virus IE63 protein represses the basal transcription RT machinery by disorganizing the pre-initiation complex."; RL Biol. Chem. 386:255-267(2005). RN [7] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-268, AND IDENTIFICATION BY RP 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 [8] 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 [9] RP INTERACTION WITH ATF7IP. RX PubMed=19106100; DOI=10.1074/jbc.m807098200; RA Liu L., Ishihara K., Ichimura T., Fujita N., Hino S., Tomita S., RA Watanabe S., Saitoh N., Ito T., Nakao M.; RT "MCAF1/AM is involved in Sp1-mediated maintenance of cancer-associated RT telomerase activity."; RL J. Biol. Chem. 284:5165-5174(2009). RN [10] RP ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-67, AND IDENTIFICATION BY MASS RP SPECTROMETRY [LARGE SCALE ANALYSIS]. RX PubMed=19608861; DOI=10.1126/science.1175371; RA Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T.C., RA Olsen J.V., Mann M.; RT "Lysine acetylation targets protein complexes and co-regulates major RT cellular functions."; RL Science 325:834-840(2009). RN [11] 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 [12] 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 [13] RP STRUCTURE BY ELECTRON MICROSCOPY (3.90 ANGSTROMS) IN COMPLEX WITH ZN(2+), RP 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). CC -!- FUNCTION: Recruits TFIIH to the initiation complex and stimulates the CC RNA polymerase II C-terminal domain kinase and DNA-dependent ATPase CC activities of TFIIH. Both TFIIH and TFIIE are required for promoter CC clearance by RNA polymerase. CC -!- SUBUNIT: Tetramer of two alpha and two beta chains (PubMed:1956398). CC Interacts with TAF6/TAFII80 (PubMed:7667268). Interacts with ATF7IP CC (PubMed:19106100). Interacts with SND1 (PubMed:7651391). Part of TBP- CC based Pol II pre-initiation complex (PIC), in which Pol II core CC assembles with general transcription factors and other specific CC initiation factors including GTF2E1, GTF2E2, GTF2F1, GTF2F2, TCEA1, CC ERCC2, ERCC3, GTF2H2, GTF2H3, GTF2H4, GTF2H5, GTF2A1, GTF2A2, GTF2B and CC TBP; this large multi-subunit PIC complex mediates DNA unwinding and CC targets Pol II core to the transcription start site where the first CC phosphodiester bond forms. {ECO:0000269|PubMed:19106100, CC ECO:0000269|PubMed:1956398, ECO:0000269|PubMed:7651391, CC ECO:0000269|PubMed:7667268, ECO:0000269|Ref.3}. CC -!- SUBUNIT: (Microbial infection) Interacts with varicella-zoster virus CC IE63 protein. {ECO:0000269|PubMed:15843171}. CC -!- INTERACTION: CC P29083; P29084: GTF2E2; NbExp=9; IntAct=EBI-5462215, EBI-2853321; CC P29083; P32780: GTF2H1; NbExp=21; IntAct=EBI-5462215, EBI-715539; CC P29083; Q7Z6K4: NRARP; NbExp=3; IntAct=EBI-5462215, EBI-5773228; CC P29083; Q8IYX1: TBC1D21; NbExp=3; IntAct=EBI-5462215, EBI-12018146; CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:1956398, CC ECO:0000269|PubMed:7651391}. CC -!- SIMILARITY: Belongs to the TFIIE alpha subunit family. {ECO:0000305}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; S67859; AAB20413.1; -; mRNA. DR EMBL; X63468; CAA45068.1; -; mRNA. DR CCDS; CCDS3002.1; -. DR PIR; S29291; S29291. DR RefSeq; NP_005504.2; NM_005513.3. DR PDB; 1VD4; NMR; -; A=113-174. DR PDB; 2JTX; NMR; -; A=336-439. DR PDB; 2RNQ; NMR; -; A=378-439. DR PDB; 2RNR; NMR; -; A=378-439. DR PDB; 5GPY; X-ray; 2.10 A; A=1-217. DR PDB; 5IY6; EM; 7.20 A; Q=1-439. DR PDB; 5IY7; EM; 8.60 A; Q=1-439. DR PDB; 5IY8; EM; 7.90 A; Q=1-439. DR PDB; 5IY9; EM; 6.30 A; Q=1-439. DR PDB; 5IYA; EM; 5.40 A; Q=1-439. DR PDB; 5IYB; EM; 3.90 A; Q=1-439. DR PDB; 5IYC; EM; 3.90 A; Q=1-439. DR PDB; 5IYD; EM; 3.90 A; Q=1-439. DR PDB; 6O9L; EM; 7.20 A; Q=1-439. DR PDB; 7EG9; EM; 3.70 A; U=1-439. DR PDB; 7EGA; EM; 4.10 A; U=1-439. DR PDB; 7EGB; EM; 3.30 A; U=1-439. DR PDB; 7EGC; EM; 3.90 A; U=1-439. DR PDB; 7ENA; EM; 4.07 A; EA=1-439. DR PDB; 7ENC; EM; 4.13 A; EA=1-439. DR PDB; 7LBM; EM; 4.80 A; Q=1-439. DR PDB; 7NVR; EM; 4.50 A; W=1-439. DR PDB; 7NVS; EM; 2.80 A; W=1-439. DR PDB; 7NVT; EM; 2.90 A; W=1-439. DR PDB; 7NVU; EM; 2.50 A; W=1-439. DR PDB; 7NVV; EM; 2.90 A; W=1-439. DR PDB; 7NVW; EM; 4.30 A; W=1-439. DR PDB; 7NVX; EM; 3.90 A; W=1-439. DR PDB; 7NVY; EM; 7.30 A; W=1-439. DR PDB; 7NVZ; EM; 7.20 A; W=1-439. DR PDB; 7NW0; EM; 6.60 A; W=1-439. DR PDB; 8BVW; EM; 4.00 A; W=1-439. DR PDB; 8BYQ; EM; 4.10 A; W=1-196. DR PDB; 8GXQ; EM; 5.04 A; EA=1-439. DR PDB; 8GXS; EM; 4.16 A; EA=1-439. DR PDB; 8S51; EM; 3.10 A; W=1-439. DR PDB; 8S52; EM; 2.90 A; W=1-439. DR PDB; 8S54; EM; 3.40 A; W=1-439. DR PDB; 8S55; EM; 3.40 A; W=1-439. DR PDB; 8S5N; EM; 3.40 A; W=1-439. DR PDB; 8WAK; EM; 5.47 A; U=1-439. DR PDB; 8WAL; EM; 8.52 A; U=1-439. DR PDB; 8WAN; EM; 6.07 A; U=1-439. DR PDB; 8WAO; EM; 6.40 A; U=1-439. DR PDB; 8WAP; EM; 5.85 A; U=1-439. DR PDB; 8WAQ; EM; 6.29 A; U=1-439. DR PDB; 8WAR; EM; 7.20 A; U=1-439. DR PDB; 8WAS; EM; 6.13 A; U=1-439. DR AlphaFoldDB; P29083; -. DR EMDB; EMD-12610; -. DR EMDB; EMD-12611; -. DR EMDB; EMD-12612; -. DR EMDB; EMD-12613; -. DR EMDB; EMD-12614; -. DR EMDB; EMD-12615; -. DR EMDB; EMD-12616; -. DR EMDB; EMD-12617; -. DR EMDB; EMD-12618; -. DR EMDB; EMD-12619; -. DR EMDB; EMD-16274; -. DR EMDB; EMD-16331; -. DR EMDB; EMD-19718; -. DR EMDB; EMD-19719; -. DR EMDB; EMD-19720; -. DR EMDB; EMD-19726; -. DR EMDB; EMD-19743; -. DR EMDB; EMD-23255; -. DR EMDB; EMD-31109; -. DR EMDB; EMD-31110; -. DR EMDB; EMD-31111; -. DR EMDB; EMD-31112; -. DR EMDB; EMD-31204; -. DR EMDB; EMD-31207; -. DR EMDB; EMD-34359; -. DR EMDB; EMD-34360; -. DR EMDB; EMD-37395; -. DR EMDB; EMD-37396; -. DR EMDB; EMD-37398; -. DR EMDB; EMD-37399; -. DR EMDB; EMD-37400; -. DR EMDB; EMD-37401; -. DR EMDB; EMD-37402; -. DR EMDB; EMD-37403; -. 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 SMR; P29083; -. DR BioGRID; 109215; 150. DR ComplexPortal; CPX-2394; General transcription factor TFIIE complex. DR CORUM; P29083; -. DR DIP; DIP-717N; -. DR FunCoup; P29083; 3877. DR IntAct; P29083; 31. DR MINT; P29083; -. DR NDEx; IQUERY-CP-GTF2E1; 2 NDEx IQuery Curated Pathways. DR STRING; 9606.ENSP00000283875; -. DR GlyGen; P29083; 1 site, 1 O-linked glycan (1 site). DR iPTMnet; P29083; -. DR PhosphoSitePlus; P29083; -. DR BioMuta; GTF2E1; -. DR DMDM; 116242812; -. DR jPOST; P29083; -. DR MassIVE; P29083; -. DR PaxDb; 9606-ENSP00000283875; -. DR PeptideAtlas; P29083; -. DR ProteomicsDB; 54517; -. DR Pumba; P29083; -. DR Antibodypedia; 4082; 208 antibodies from 31 providers. DR DNASU; 2960; -. DR Ensembl; ENST00000283875.6; ENSP00000283875.5; ENSG00000153767.11. DR Ensembl; ENST00000881964.1; ENSP00000552023.1; ENSG00000153767.11. DR Ensembl; ENST00000881966.1; ENSP00000552025.1; ENSG00000153767.11. DR Ensembl; ENST00000932500.1; ENSP00000602559.1; ENSG00000153767.11. DR Ensembl; ENST00000932501.1; ENSP00000602560.1; ENSG00000153767.11. DR Ensembl; ENST00000932503.1; ENSP00000602562.1; ENSG00000153767.11. DR Ensembl; ENST00000932504.1; ENSP00000602563.1; ENSG00000153767.11. DR Ensembl; ENST00000932505.1; ENSP00000602564.1; ENSG00000153767.11. DR Ensembl; ENST00000932506.1; ENSP00000602565.1; ENSG00000153767.11. DR Ensembl; ENST00000932507.1; ENSP00000602566.1; ENSG00000153767.11. DR Ensembl; ENST00000932509.1; ENSP00000602568.1; ENSG00000153767.11. DR Ensembl; ENST00000932510.1; ENSP00000602569.1; ENSG00000153767.11. DR Ensembl; ENST00000959111.1; ENSP00000629170.1; ENSG00000153767.11. DR Ensembl; ENST00000959112.1; ENSP00000629171.1; ENSG00000153767.11. DR Ensembl; ENST00000959113.1; ENSP00000629172.1; ENSG00000153767.11. DR GeneID; 2960; -. DR KEGG; hsa:2960; -. DR MANE-Select; ENST00000283875.6; ENSP00000283875.5; NM_005513.3; NP_005504.2. DR UCSC; uc003edz.5; human. DR AGR; HGNC:4650; -. DR ClinPGx; PA29036; -. DR CTD; 2960; -. DR DisGeNET; 2960; -. DR GeneCards; GTF2E1; -. DR HGNC; HGNC:4650; GTF2E1. DR HPA; ENSG00000153767; Low tissue specificity. DR MIM; 189962; gene. DR OpenTargets; ENSG00000153767; -. DR VEuPathDB; HostDB:ENSG00000153767; -. DR eggNOG; KOG2593; Eukaryota. DR GeneTree; ENSGT00390000016696; -. DR HOGENOM; CLU_051021_1_0_1; -. DR InParanoid; P29083; -. DR OMA; DAIKWKV; -. DR OrthoDB; 361102at2759; -. DR PAN-GO; P29083; 2 GO annotations based on evolutionary models. DR PhylomeDB; P29083; -. DR PathwayCommons; P29083; -. 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 SignaLink; P29083; -. DR SIGNOR; P29083; -. DR Agora; ENSG00000153767; -. DR BioGRID-ORCS; 2960; 733 hits in 1173 CRISPR screens. DR ChiTaRS; GTF2E1; human. DR EvolutionaryTrace; P29083; -. DR GeneWiki; GTF2E1; -. DR GenomeRNAi; 2960; -. DR Pharos; P29083; Tbio. DR PRO; PR:P29083; -. DR Proteomes; UP000005640; Chromosome 3. DR RNAct; P29083; protein. DR Bgee; ENSG00000153767; Expressed in oocyte and 188 other cell types or tissues. DR ExpressionAtlas; P29083; baseline and differential. DR GO; GO:0005654; C:nucleoplasm; IDA:HPA. DR GO; GO:0005634; C:nucleus; IDA:CAFA. DR GO; GO:0005669; C:transcription factor TFIID complex; IDA:UniProtKB. DR GO; GO:0005673; C:transcription factor TFIIE complex; IPI:ComplexPortal. DR GO; GO:0016251; F:RNA polymerase II general transcription initiation factor activity; IDA:ARUK-UCL. DR GO; GO:0051123; P:RNA polymerase II preinitiation complex assembly; IDA:ComplexPortal. DR GO; GO:0006366; P:transcription by RNA polymerase II; IDA:ARUK-UCL. DR GO; GO:0006367; P:transcription initiation at RNA polymerase II promoter; IBA:GO_Central. DR DisProt; DP01633; -. DR FunFam; 3.30.40.10:FF:000087; General transcription factor IIE subunit 1; 1. DR Gene3D; 6.10.140.1250; -; 1. DR Gene3D; 3.30.40.10; Zinc/RING finger domain, C3HC4 (zinc finger); 1. DR IDEAL; IID00548; -. DR InterPro; IPR039997; TFE. DR InterPro; IPR017919; TFIIE/TFIIEa_HTH. DR InterPro; IPR002853; TFIIE_asu. DR InterPro; IPR021600; TFIIE_asu_C. DR InterPro; IPR024550; TFIIEa/SarR/Rpc3_HTH_dom. DR InterPro; IPR013083; Znf_RING/FYVE/PHD. DR InterPro; IPR013137; Znf_TFIIB. DR PANTHER; PTHR13097:SF8; GENERAL TRANSCRIPTION FACTOR IIE SUBUNIT 1; 1. DR PANTHER; PTHR13097; TRANSCRIPTION INITIATION FACTOR IIE, ALPHA SUBUNIT; 1. DR Pfam; PF11521; TFIIE-A_C; 1. DR Pfam; PF02002; TFIIE_alpha; 1. DR Pfam; PF08271; Zn_Ribbon_TF; 1. DR SMART; SM00531; TFIIE; 1. DR SUPFAM; SSF57783; Zinc beta-ribbon; 1. DR PROSITE; PS51344; HTH_TFE_IIE; 1. DR PDBsum; 1VD4; -. DR PDBsum; 2JTX; -. DR PDBsum; 2RNQ; -. DR PDBsum; 2RNR; -. DR PDBsum; 5GPY; -. 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; 6O9L; -. DR PDBsum; 7EG9; -. DR PDBsum; 7EGA; -. DR PDBsum; 7EGB; -. DR PDBsum; 7EGC; -. DR PDBsum; 7ENA; -. DR PDBsum; 7ENC; -. DR PDBsum; 7LBM; -. DR PDBsum; 7NVR; -. DR PDBsum; 7NVS; -. DR PDBsum; 7NVT; -. DR PDBsum; 7NVU; -. DR PDBsum; 7NVV; -. DR PDBsum; 7NVW; -. DR PDBsum; 7NVX; -. DR PDBsum; 7NVY; -. DR PDBsum; 7NVZ; -. DR PDBsum; 7NW0; -. DR PDBsum; 8BVW; -. DR PDBsum; 8BYQ; -. DR PDBsum; 8GXQ; -. DR PDBsum; 8GXS; -. DR PDBsum; 8S51; -. DR PDBsum; 8S52; -. DR PDBsum; 8S54; -. DR PDBsum; 8S55; -. DR PDBsum; 8S5N; -. DR PDBsum; 8WAK; -. DR PDBsum; 8WAL; -. DR PDBsum; 8WAN; -. DR PDBsum; 8WAO; -. DR PDBsum; 8WAP; -. DR PDBsum; 8WAQ; -. DR PDBsum; 8WAR; -. DR PDBsum; 8WAS; -. PE 1: Evidence at protein level; KW 3D-structure; Acetylation; Direct protein sequencing; KW Host-virus interaction; Metal-binding; Nucleus; Phosphoprotein; KW Proteomics identification; Reference proteome; Transcription; KW Transcription regulation; Zinc; Zinc-finger. FT INIT_MET 1 FT /note="Removed" FT /evidence="ECO:0000269|Ref.3, ECO:0007744|PubMed:19413330, FT ECO:0007744|PubMed:22814378" FT CHAIN 2..439 FT /note="General transcription factor IIE subunit 1" FT /id="PRO_0000211222" FT DOMAIN 14..104 FT /note="HTH TFE/IIEalpha-type" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00676" FT ZN_FING 129..157 FT /note="C4-type" FT /evidence="ECO:0000255" FT REGION 332..393 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 333..344 FT /note="Low complexity" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 354..364 FT /note="Acidic residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 379..392 FT /note="Acidic residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT BINDING 129 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /evidence="ECO:0000269|PubMed:27193682, FT ECO:0007744|PDB:5IY6" FT BINDING 132 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /evidence="ECO:0000269|PubMed:27193682, FT ECO:0007744|PDB:5IY6" FT BINDING 154 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /evidence="ECO:0000269|PubMed:27193682, FT ECO:0007744|PDB:5IY6" FT BINDING 157 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /evidence="ECO:0000269|PubMed:27193682, FT ECO:0007744|PDB:5IY6" FT MOD_RES 2 FT /note="N-acetylalanine" FT /evidence="ECO:0000269|Ref.3, ECO:0007744|PubMed:19413330, FT ECO:0007744|PubMed:22814378" FT MOD_RES 67 FT /note="N6-acetyllysine" FT /evidence="ECO:0007744|PubMed:19608861" FT MOD_RES 268 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:18669648" FT VARIANT 366 FT /note="P -> S (in dbSNP:rs3732401)" FT /id="VAR_020321" FT CONFLICT 352 FT /note="S -> D (in Ref. 2; CAA45068)" FT /evidence="ECO:0000305" FT HELIX 12..25 FT /evidence="ECO:0007829|PDB:5GPY" FT HELIX 28..39 FT /evidence="ECO:0007829|PDB:5GPY" FT STRAND 40..44 FT /evidence="ECO:0007829|PDB:5GPY" FT HELIX 45..52 FT /evidence="ECO:0007829|PDB:5GPY" FT HELIX 56..68 FT /evidence="ECO:0007829|PDB:5GPY" FT STRAND 71..80 FT /evidence="ECO:0007829|PDB:5GPY" FT STRAND 82..84 FT /evidence="ECO:0007829|PDB:8S54" FT STRAND 86..94 FT /evidence="ECO:0007829|PDB:5GPY" FT HELIX 96..122 FT /evidence="ECO:0007829|PDB:5GPY" FT STRAND 127..129 FT /evidence="ECO:0007829|PDB:7NVU" FT TURN 130..132 FT /evidence="ECO:0007829|PDB:5GPY" FT STRAND 134..136 FT /evidence="ECO:0007829|PDB:7NVU" FT HELIX 138..142 FT /evidence="ECO:0007829|PDB:5GPY" FT TURN 147..150 FT /evidence="ECO:0007829|PDB:5GPY" FT STRAND 151..153 FT /evidence="ECO:0007829|PDB:5GPY" FT TURN 155..157 FT /evidence="ECO:0007829|PDB:5GPY" FT HELIX 164..166 FT /evidence="ECO:0007829|PDB:7NVS" FT STRAND 171..173 FT /evidence="ECO:0007829|PDB:7EGB" FT HELIX 176..193 FT /evidence="ECO:0007829|PDB:5GPY" FT HELIX 276..278 FT /evidence="ECO:0007829|PDB:7NVV" FT HELIX 279..282 FT /evidence="ECO:0007829|PDB:7NVV" FT STRAND 380..383 FT /evidence="ECO:0007829|PDB:2RNQ" FT STRAND 388..390 FT /evidence="ECO:0007829|PDB:2RNR" FT HELIX 392..394 FT /evidence="ECO:0007829|PDB:2JTX" FT STRAND 395..398 FT /evidence="ECO:0007829|PDB:2JTX" FT STRAND 401..404 FT /evidence="ECO:0007829|PDB:2JTX" FT HELIX 405..410 FT /evidence="ECO:0007829|PDB:2JTX" FT HELIX 412..417 FT /evidence="ECO:0007829|PDB:2JTX" FT HELIX 420..433 FT /evidence="ECO:0007829|PDB:2JTX" SQ SEQUENCE 439 AA; 49452 MW; 9234FFE3F150340B CRC64; MADPDVLTEV PAALKRLAKY VIRGFYGIEH ALALDILIRN SCVKEEDMLE LLKFDRKQLR SVLNNLKGDK FIKCRMRVET AADGKTTRHN YYFINYRTLV NVVKYKLDHM RRRIETDERD STNRASFKCP VCSSTFTDLE ANQLFDPMTG TFRCTFCHTE VEEDESAMPK KDARTLLARF NEQIEPIYAL LRETEDVNLA YEILEPEPTE IPALKQSKDH AATTAGAASL AGGHHREAWA TKGPSYEDLY TQNVVINMDD QEDLHRASLE GKSAKERPIW LRESTVQGAY GSEDMKEGGI DMDAFQEREE GHAGPDDNEE VMRALLIHEK KTSSAMAGSV GAAAPVTAAN GSDSESETSE SDDDSPPRPA AVAVHKREED EEEDDEFEEV ADDPIVMVAG RPFSYSEVSQ RPELVAQMTP EEKEAYIAMG QRMFEDLFE //