位置:首页 > 蛋白库 > T2FB_RAT
T2FB_RAT
ID   T2FB_RAT                Reviewed;         249 AA.
AC   Q01750;
DT   01-JUL-1993, integrated into UniProtKB/Swiss-Prot.
DT   01-JUL-1993, sequence version 1.
DT   03-AUG-2022, entry version 140.
DE   RecName: Full=General transcription factor IIF subunit 2;
DE   AltName: Full=Transcription initiation factor IIF subunit beta;
DE            Short=TFIIF-beta;
DE   AltName: Full=Transcription initiation factor RAP30;
GN   Name=Gtf2f2; Synonyms=Rap30;
OS   Rattus norvegicus (Rat).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC   Murinae; Rattus.
OX   NCBI_TaxID=10116;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RX   PubMed=1429731; DOI=10.1016/s0021-9258(18)35928-3;
RA   Garrett K.P., Serizawa H., Hanley J.P., Bradsher J.N., Tsuboi A., Arai N.,
RA   Yokota T., Arai K., Conaway R.C., Conaway J.W.;
RT   "The carboxyl terminus of RAP30 is similar in sequence to region 4 of
RT   bacterial sigma factors and is required for function.";
RL   J. Biol. Chem. 267:23942-23949(1992).
RN   [2]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-248, AND IDENTIFICATION BY
RP   MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX   PubMed=22673903; DOI=10.1038/ncomms1871;
RA   Lundby A., Secher A., Lage K., Nordsborg N.B., Dmytriyev A., Lundby C.,
RA   Olsen J.V.;
RT   "Quantitative maps of protein phosphorylation sites across 14 different rat
RT   organs and tissues.";
RL   Nat. Commun. 3:876-876(2012).
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. It promotes transcription elongation.
CC       {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|UniProtKB:P13984}.
CC   -!- SUBCELLULAR LOCATION: Nucleus.
CC   -!- SIMILARITY: Belongs to the TFIIF beta 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; L01267; AAA42005.1; -; mRNA.
DR   AlphaFoldDB; Q01750; -.
DR   SMR; Q01750; -.
DR   STRING; 10116.ENSRNOP00000044668; -.
DR   iPTMnet; Q01750; -.
DR   PhosphoSitePlus; Q01750; -.
DR   PaxDb; Q01750; -.
DR   PRIDE; Q01750; -.
DR   UCSC; RGD:620772; rat.
DR   RGD; 620772; Gtf2f2.
DR   eggNOG; KOG2905; Eukaryota.
DR   InParanoid; Q01750; -.
DR   PhylomeDB; Q01750; -.
DR   Reactome; R-RNO-112382; Formation of RNA Pol II elongation complex.
DR   Reactome; R-RNO-113418; Formation of the Early Elongation Complex.
DR   Reactome; R-RNO-674695; RNA Polymerase II Pre-transcription Events.
DR   Reactome; R-RNO-6796648; TP53 Regulates Transcription of DNA Repair Genes.
DR   Reactome; R-RNO-6803529; FGFR2 alternative splicing.
DR   Reactome; R-RNO-6807505; RNA polymerase II transcribes snRNA genes.
DR   Reactome; R-RNO-72086; mRNA Capping.
DR   Reactome; R-RNO-72163; mRNA Splicing - Major Pathway.
DR   Reactome; R-RNO-72165; mRNA Splicing - Minor Pathway.
DR   Reactome; R-RNO-72203; Processing of Capped Intron-Containing Pre-mRNA.
DR   Reactome; R-RNO-73776; RNA Polymerase II Promoter Escape.
DR   Reactome; R-RNO-73779; RNA Polymerase II Transcription Pre-Initiation And Promoter Opening.
DR   Reactome; R-RNO-75953; RNA Polymerase II Transcription Initiation.
DR   Reactome; R-RNO-75955; RNA Polymerase II Transcription Elongation.
DR   Reactome; R-RNO-76042; RNA Polymerase II Transcription Initiation And Promoter Clearance.
DR   Reactome; R-RNO-77075; RNA Pol II CTD phosphorylation and interaction with CE.
DR   Reactome; R-RNO-9018519; Estrogen-dependent gene expression.
DR   PRO; PR:Q01750; -.
DR   Proteomes; UP000002494; Unplaced.
DR   GO; GO:0005634; C:nucleus; ISO:RGD.
DR   GO; GO:0005674; C:transcription factor TFIIF complex; ISO:RGD.
DR   GO; GO:0005675; C:transcription factor TFIIH holo complex; IDA:RGD.
DR   GO; GO:0097550; C:transcription preinitiation complex; ISO:RGD.
DR   GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
DR   GO; GO:0003678; F:DNA helicase activity; IEA:UniProtKB-EC.
DR   GO; GO:0016251; F:RNA polymerase II general transcription initiation factor activity; IDA:ARUK-UCL.
DR   GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; ISO:RGD.
DR   GO; GO:0051123; P:RNA polymerase II preinitiation complex assembly; IDA:RGD.
DR   GO; GO:0006366; P:transcription by RNA polymerase II; IDA:RGD.
DR   GO; GO:0006368; P:transcription elongation from RNA polymerase II promoter; IDA:RGD.
DR   GO; GO:0006367; P:transcription initiation from RNA polymerase II promoter; IDA:ARUK-UCL.
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   1: Evidence at protein 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_0000211237"
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:0007744|PubMed:22673903"
SQ   SEQUENCE   249 AA;  28349 MW;  5299CAD9AF454A91 CRC64;
     MAERGELDLT GAKQNTGVWL VKVPKYLSQQ WAKAPGRGEV GKLRIAKNQG RTEVSFTLNE
     DLANIHDIGG KPASVSAPRE HPFVLQSVGG QTLTVFTESS SDKLSLEGIV VQRAECRPAA
     SENYMKLKRL QIEESSKPVR LSQQADKVVT TNYKPVANHQ YNIEYERKKK EDGKRARADK
     QHVLDMLFSA FEKHQYYNLK DLVDITKQPV GYLKEILKEI GIQNVKGIHK NTWELKPEYR
     HYQTEEKSD
 
 
维奥蛋白资源库 - 中文蛋白资源 CopyRight © 2010-2024