T2EA_HUMAN
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 03-AUG-2022, entry version 204.
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).
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).
CC {ECO:0000269|PubMed:19106100, ECO:0000269|PubMed:1956398,
CC ECO:0000269|PubMed:7651391, ECO:0000269|PubMed:7667268}.
CC -!- SUBUNIT: (Microbial infection) Interacts with varicella-zoster virus
CC IE63 protein. {ECO:0000269|PubMed:15843171}.
CC -!- INTERACTION:
CC P29083; P29084: GTF2E2; NbExp=6; 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}.
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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_005513.2.
DR RefSeq; XP_011511046.1; XM_011512744.2.
DR RefSeq; XP_011511047.1; XM_011512745.2.
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 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 AlphaFoldDB; P29083; -.
DR SMR; P29083; -.
DR BioGRID; 109215; 123.
DR CORUM; P29083; -.
DR DIP; DIP-717N; -.
DR IntAct; P29083; 23.
DR MINT; P29083; -.
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 EPD; P29083; -.
DR jPOST; P29083; -.
DR MassIVE; P29083; -.
DR MaxQB; P29083; -.
DR PaxDb; P29083; -.
DR PeptideAtlas; P29083; -.
DR PRIDE; P29083; -.
DR ProteomicsDB; 54517; -.
DR Antibodypedia; 4082; 195 antibodies from 29 providers.
DR DNASU; 2960; -.
DR Ensembl; ENST00000283875.6; ENSP00000283875.5; ENSG00000153767.10.
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 CTD; 2960; -.
DR GeneCards; GTF2E1; -.
DR HGNC; HGNC:4650; GTF2E1.
DR HPA; ENSG00000153767; Low tissue specificity.
DR MIM; 189962; gene.
DR neXtProt; NX_P29083; -.
DR OpenTargets; ENSG00000153767; -.
DR PharmGKB; PA29036; -.
DR VEuPathDB; HostDB:ENSG00000153767; -.
DR eggNOG; KOG2593; Eukaryota.
DR GeneTree; ENSGT00390000016696; -.
DR HOGENOM; CLU_051021_1_0_1; -.
DR InParanoid; P29083; -.
DR OMA; EYYSHMY; -.
DR OrthoDB; 1343016at2759; -.
DR PhylomeDB; P29083; -.
DR TreeFam; TF313429; -.
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 BioGRID-ORCS; 2960; 721 hits in 1086 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 187 other tissues.
DR ExpressionAtlas; P29083; baseline and differential.
DR Genevisible; P29083; HS.
DR GO; GO:0005829; C:cytosol; IDA:HPA.
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; IBA:GO_Central.
DR GO; GO:0097550; C:transcription preinitiation complex; IDA:CAFA.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0016251; F:RNA polymerase II general transcription initiation factor activity; IDA:ARUK-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; TAS:ProtInc.
DR GO; GO:0001113; P:transcription open complex formation at RNA polymerase II promoter; IBA:GO_Central.
DR DisProt; DP01633; -.
DR Gene3D; 3.30.40.10; -; 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; PTHR13097; 1.
DR Pfam; PF08271; TF_Zn_Ribbon; 1.
DR Pfam; PF11521; TFIIE-A_C; 1.
DR Pfam; PF02002; TFIIE_alpha; 1.
DR SMART; SM00531; TFIIE; 1.
DR PROSITE; PS51344; HTH_TFE_IIE; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Acetylation; Direct protein sequencing;
KW Host-virus interaction; Metal-binding; Nucleus; Phosphoprotein;
KW Reference proteome; Transcription; Transcription regulation; Zinc;
KW 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 361..378
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
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 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..149
FT /evidence="ECO:0007829|PDB:5GPY"
FT STRAND 150..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 HELIX 176..193
FT /evidence="ECO:0007829|PDB:5GPY"
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 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
