ID   T2EB_BOVIN              Reviewed;         289 AA.
AC   Q2KJF9;
DT   28-NOV-2006, integrated into UniProtKB/Swiss-Prot.
DT   07-MAR-2006, sequence version 1.
DT   25-MAY-2022, entry version 85.
DE   RecName: Full=General transcription factor IIE subunit 2;
DE   AltName: Full=Transcription initiation factor IIE subunit beta;
DE            Short=TFIIE-beta;
GN   Name=GTF2E2;
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=Crossbred X Angus; TISSUE=Liver;
RG   NIH - Mammalian Gene Collection (MGC) project;
RL   Submitted (SEP-2005) 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 FACT
CC       subunit SUPT16H. Interacts with ATF7IP. Interacts with SND1.
CC       {ECO:0000250|UniProtKB:P29084}.
CC   -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000255|PROSITE-ProRule:PRU00682}.
CC   -!- SIMILARITY: Belongs to the TFIIE beta subunit family.
CC       {ECO:0000255|PROSITE-ProRule:PRU00682}.
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DR   EMBL; BC105362; AAI05363.1; -; mRNA.
DR   RefSeq; NP_001039530.1; NM_001046065.2.
DR   AlphaFoldDB; Q2KJF9; -.
DR   SMR; Q2KJF9; -.
DR   STRING; 9913.ENSBTAP00000016863; -.
DR   PaxDb; Q2KJF9; -.
DR   PRIDE; Q2KJF9; -.
DR   GeneID; 510921; -.
DR   KEGG; bta:510921; -.
DR   CTD; 2961; -.
DR   eggNOG; KOG3095; Eukaryota.
DR   InParanoid; Q2KJF9; -.
DR   OrthoDB; 1160863at2759; -.
DR   Proteomes; UP000009136; Unplaced.
DR   GO; GO:0005673; C:transcription factor TFIIE complex; IEA:InterPro.
DR   GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
DR   GO; GO:0006367; P:transcription initiation from RNA polymerase II promoter; IEA:InterPro.
DR   CDD; cd07977; TFIIE_beta_winged_helix; 1.
DR   Gene3D; 1.10.10.10; -; 1.
DR   InterPro; IPR040501; TFA2_Winged_2.
DR   InterPro; IPR016656; TFIIE-bsu.
DR   InterPro; IPR003166; TFIIE_bsu_DNA-bd.
DR   InterPro; IPR036388; WH-like_DNA-bd_sf.
DR   InterPro; IPR036390; WH_DNA-bd_sf.
DR   PANTHER; PTHR12716; PTHR12716; 1.
DR   Pfam; PF18121; TFA2_Winged_2; 1.
DR   Pfam; PF02186; TFIIE_beta; 1.
DR   PIRSF; PIRSF016398; TFIIE-beta; 1.
DR   SUPFAM; SSF46785; SSF46785; 1.
DR   PROSITE; PS51351; TFIIE_BETA_C; 1.
PE   2: Evidence at transcript level;
KW   Acetylation; DNA-binding; Nucleus; Phosphoprotein; Reference proteome;
KW   Transcription; Transcription regulation.
FT   CHAIN           1..289
FT                   /note="General transcription factor IIE subunit 2"
FT                   /id="PRO_0000260325"
FT   DNA_BIND        64..144
FT                   /note="TFIIE beta"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00682"
FT   REGION          17..61
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          242..274
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        29..44
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        45..61
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        253..271
FT                   /note="Basic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOD_RES         1
FT                   /note="N-acetylmethionine"
FT                   /evidence="ECO:0000250|UniProtKB:P29084"
FT   MOD_RES         59
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:P29084"
FT   MOD_RES         72
FT                   /note="N6-acetyllysine"
FT                   /evidence="ECO:0000250|UniProtKB:Q9D902"
SQ   SEQUENCE   289 AA;  32731 MW;  587B7472C17A6BFF CRC64;
     MDPSLLRERE LFKKRALSTP AVEKRSVSSE ASSSKKKKAK LEHGGSSGSK QNSDHSNGSF
     NLKALSGSSG YKFGVLAKIV NYMKTRHQRG DTHPLTLEEI LDETQHLDIG LKQKQWLMSE
     ALVNNPKIEV VDGKYAFKPK YNLKDKKALL RLLDQHDQRG LGGILLEDIE EGLPNSQKAV
     KALGDQILFV NRPDKKKILF FNDKSCQFSV DEEFQKLWRS VTVDSMDEEK IEEYLKRQGI
     SSMQDSGPKK VAPIQRRKKP ASQKKRRFKT HNEHLAGVLK DYSDIAPGK