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T2FB_BOVIN
ID   T2FB_BOVIN              Reviewed;         249 AA.
AC   Q2T9L9;
DT   28-NOV-2006, integrated into UniProtKB/Swiss-Prot.
DT   24-JAN-2006, sequence version 1.
DT   03-AUG-2022, entry version 120.
DE   RecName: Full=General transcription factor IIF subunit 2;
DE   AltName: Full=Transcription initiation factor IIF subunit beta;
DE            Short=TFIIF-beta;
GN   Name=GTF2F2;
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 (DEC-2005) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: TFIIF is a general transcription initiation factor that binds
CC       to RNA polymerase II and helps to recruit it to the initiation complex
CC       in collaboration with TFIIB. {ECO:0000250|UniProtKB:P13984}.
CC   -!- SUBUNIT: Heterodimer of an alpha and a beta subunit. Interacts with
CC       HTATSF1, GPBP1 and URI1 (By similarity). Interacts with GTF2B (via N-
CC       terminus); this interaction is inhibited in presence of GTF2F1 (By
CC       similarity). {ECO:0000250, ECO:0000250|UniProtKB:P13984}.
CC   -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the TFIIF beta subunit family. {ECO:0000305}.
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DR   EMBL; BC111360; AAI11361.1; -; mRNA.
DR   RefSeq; NP_001033153.1; NM_001038064.1.
DR   AlphaFoldDB; Q2T9L9; -.
DR   SMR; Q2T9L9; -.
DR   STRING; 9913.ENSBTAP00000045836; -.
DR   PaxDb; Q2T9L9; -.
DR   PRIDE; Q2T9L9; -.
DR   Ensembl; ENSBTAT00000048870; ENSBTAP00000045836; ENSBTAG00000034495.
DR   Ensembl; ENSBTAT00000078070; ENSBTAP00000061447; ENSBTAG00000049772.
DR   GeneID; 509259; -.
DR   KEGG; bta:509259; -.
DR   CTD; 2963; -.
DR   VEuPathDB; HostDB:ENSBTAG00000034495; -.
DR   VEuPathDB; HostDB:ENSBTAG00000049772; -.
DR   VGNC; VGNC:53815; GTF2F2.
DR   eggNOG; KOG2905; Eukaryota.
DR   GeneTree; ENSGT00390000016051; -.
DR   HOGENOM; CLU_047858_1_0_1; -.
DR   InParanoid; Q2T9L9; -.
DR   OMA; KYIANKW; -.
DR   OrthoDB; 1496393at2759; -.
DR   TreeFam; TF314290; -.
DR   Reactome; R-BTA-113418; Formation of the Early Elongation Complex.
DR   Reactome; R-BTA-674695; RNA Polymerase II Pre-transcription Events.
DR   Proteomes; UP000009136; Chromosome 12.
DR   Proteomes; UP000009136; Chromosome 13.
DR   Bgee; ENSBTAG00000034495; Expressed in oocyte and 105 other tissues.
DR   GO; GO:0005674; C:transcription factor TFIIF complex; IBA:GO_Central.
DR   GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
DR   GO; GO:0003678; F:DNA helicase activity; IEA:UniProtKB-EC.
DR   GO; GO:0006366; P:transcription by RNA polymerase II; ISS:UniProtKB.
DR   GO; GO:0006367; P:transcription initiation from RNA polymerase II promoter; IBA:GO_Central.
DR   Gene3D; 1.10.10.10; -; 1.
DR   InterPro; IPR003196; TFIIF_beta.
DR   InterPro; IPR040450; TFIIF_beta_HTH.
DR   InterPro; IPR040504; TFIIF_beta_N.
DR   InterPro; IPR011039; TFIIF_interaction.
DR   InterPro; IPR036388; WH-like_DNA-bd_sf.
DR   InterPro; IPR036390; WH_DNA-bd_sf.
DR   PANTHER; PTHR10445; PTHR10445; 1.
DR   Pfam; PF02270; TFIIF_beta; 1.
DR   Pfam; PF17683; TFIIF_beta_N; 1.
DR   PIRSF; PIRSF015849; TFIIF-beta; 1.
DR   SUPFAM; SSF46785; SSF46785; 1.
DR   SUPFAM; SSF50916; SSF50916; 1.
PE   2: Evidence at transcript level;
KW   Acetylation; DNA-binding; Nucleus; Phosphoprotein; Reference proteome;
KW   Transcription; Transcription regulation.
FT   INIT_MET        1
FT                   /note="Removed"
FT                   /evidence="ECO:0000250|UniProtKB:P13984"
FT   CHAIN           2..249
FT                   /note="General transcription factor IIF subunit 2"
FT                   /id="PRO_0000260320"
FT   MOD_RES         2
FT                   /note="N-acetylalanine"
FT                   /evidence="ECO:0000250|UniProtKB:P13984"
FT   MOD_RES         22
FT                   /note="N6-acetyllysine"
FT                   /evidence="ECO:0000250|UniProtKB:P13984"
FT   MOD_RES         33
FT                   /note="N6-acetyllysine"
FT                   /evidence="ECO:0000250|UniProtKB:P13984"
FT   MOD_RES         137
FT                   /note="N6-acetyllysine"
FT                   /evidence="ECO:0000250|UniProtKB:P13984"
FT   MOD_RES         142
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:P13984"
FT   MOD_RES         248
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:P13984"
SQ   SEQUENCE   249 AA;  28446 MW;  E2C30D0C0DE7B795 CRC64;
     MAERGELDLT GAKQNTGVWL VKVPKYLSQQ WAKAPGRGEV GKLRIAKNQG RTEVSFTLNE
     DLANIHDIGG KPASVSAPRE HPFVLQSVGG QTLTVFTESS SDKLSLEGIV VQRAECRPAA
     NENYMRLKRL QIEESSKPVR LSQQLDKVVT TNYKPVANHQ YNIEYERKKK EDGKRARADK
     QHVLDMLFSA FEKHQYYNLK DLVDITKQPV SYLKDILKEI GVQNVKGIHK NTWELKPEYR
     HYQVEEKSD
 
 
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