T2EA_BOVIN
ID T2EA_BOVIN Reviewed; 438 AA.
AC A6QLI8;
DT 26-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT 21-AUG-2007, sequence version 1.
DT 03-AUG-2022, entry version 89.
DE RecName: Full=General transcription factor IIE subunit 1;
DE AltName: Full=Transcription initiation factor IIE subunit alpha;
DE Short=TFIIE-alpha;
GN Name=GTF2E1;
OS Bos taurus (Bovine).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC Bovinae; Bos.
OX NCBI_TaxID=9913;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=Hereford; TISSUE=Basal ganglia;
RG NIH - Mammalian Gene Collection (MGC) project;
RL Submitted (JUN-2007) to the EMBL/GenBank/DDBJ databases.
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 (By similarity). {ECO:0000250}.
CC -!- SUBUNIT: Tetramer of two alpha and two beta chains. Interacts with
CC TAF6/TAFII80. Interacts with ATF7IP. Interacts with SND1.
CC {ECO:0000250|UniProtKB:P29083}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:P29083}.
CC -!- SIMILARITY: Belongs to the TFIIE alpha subunit family. {ECO:0000305}.
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DR EMBL; BC147980; AAI47981.1; -; mRNA.
DR RefSeq; NP_001096764.1; NM_001103294.1.
DR AlphaFoldDB; A6QLI8; -.
DR SMR; A6QLI8; -.
DR STRING; 9913.ENSBTAP00000050375; -.
DR PRIDE; A6QLI8; -.
DR Ensembl; ENSBTAT00000055844; ENSBTAP00000050375; ENSBTAG00000016848.
DR GeneID; 540525; -.
DR KEGG; bta:540525; -.
DR CTD; 2960; -.
DR VEuPathDB; HostDB:ENSBTAG00000016848; -.
DR VGNC; VGNC:58356; GTF2E1.
DR eggNOG; KOG2593; Eukaryota.
DR GeneTree; ENSGT00390000016696; -.
DR InParanoid; A6QLI8; -.
DR OMA; EYYSHMY; -.
DR OrthoDB; 1343016at2759; -.
DR Proteomes; UP000009136; Chromosome 1.
DR Bgee; ENSBTAG00000016848; Expressed in gluteal muscle and 106 other tissues.
DR ExpressionAtlas; A6QLI8; baseline and differential.
DR GO; GO:0005673; C:transcription factor TFIIE complex; IBA:GO_Central.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0001113; P:transcription open complex formation at RNA polymerase II promoter; IBA:GO_Central.
DR Gene3D; 3.30.40.10; -; 1.
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 2: Evidence at transcript level;
KW Acetylation; Metal-binding; Nucleus; Phosphoprotein; Reference proteome;
KW Transcription; Transcription regulation; Zinc; Zinc-finger.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000250|UniProtKB:P29083"
FT CHAIN 2..438
FT /note="General transcription factor IIE subunit 1"
FT /id="PRO_0000318949"
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 330..388
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 2
FT /note="N-acetylalanine"
FT /evidence="ECO:0000250|UniProtKB:P29083"
FT MOD_RES 67
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:P29083"
FT MOD_RES 268
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P29083"
SQ SEQUENCE 438 AA; 49211 MW; A0243821FC3FD720 CRC64;
MADPDVLTEV PAALKRLAKY VIRGFYGIEH ALALDILIRN PCVKEEDMLE LLKFDRKQLR
SVLNNLKGDK FIKCRMRVET AADGKTTRHN YYFINYRTLV NVVKYKLDHM RRRIETDERD
STNRASFKCP VCSSTFTDLE ANQLFDPMTG TFRCTFCQTE VEEDESAMPK KDARTLLARF
NEQIEPIYAL LRETEDVNLA YEILEPEPTE IPALKQSKDR AATAAGAAGL AGGHHREAWT
TKGPSYEDLY TQNVVINMDD QEDLHRASLE GKSAKERPIW LRESTVQGAY NSEEMKEGGI
DIDSFQEHEE GHAGPDDNEE VMRALLIHEK KTPSAPAGSV GAAAPVTAAN GSDSESETSE
SDDDSPPRVA TVAAHHGEED EEDDEFEEVA DDPVVMVAGR PFSYSEVSQK PELVAQMTPE
EKEAYIAMGQ RMFEDLFE