T2FB_YEAST
ID T2FB_YEAST Reviewed; 400 AA.
AC P41896; D6VUE2;
DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-1996, sequence version 2.
DT 03-AUG-2022, entry version 186.
DE RecName: Full=Transcription initiation factor IIF subunit beta;
DE AltName: Full=TFIIF medium subunit;
DE AltName: Full=TFIIF-beta;
DE AltName: Full=Transcription factor G 54 kDa subunit;
GN Name=TFG2; OrderedLocusNames=YGR005C;
OS Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Saccharomycetaceae; Saccharomyces.
OX NCBI_TaxID=559292;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND PROTEIN SEQUENCE OF 250-279 AND
RP 349-356.
RC STRAIN=ATCC 208279 / BJ926;
RX PubMed=7995524; DOI=10.1101/gad.8.23.2868;
RA Henry N.L., Campbell A.M., Feaver W.J., Poon D., Weil P.A., Kornberg R.D.;
RT "TFIIF-TAF-RNA polymerase II connection.";
RL Genes Dev. 8:2868-2878(1994).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=9169869;
RA Tettelin H., Agostoni-Carbone M.L., Albermann K., Albers M., Arroyo J.,
RA Backes U., Barreiros T., Bertani I., Bjourson A.J., Brueckner M.,
RA Bruschi C.V., Carignani G., Castagnoli L., Cerdan E., Clemente M.L.,
RA Coblenz A., Coglievina M., Coissac E., Defoor E., Del Bino S., Delius H.,
RA Delneri D., de Wergifosse P., Dujon B., Durand P., Entian K.-D., Eraso P.,
RA Escribano V., Fabiani L., Fartmann B., Feroli F., Feuermann M.,
RA Frontali L., Garcia-Gonzalez M., Garcia-Saez M.I., Goffeau A.,
RA Guerreiro P., Hani J., Hansen M., Hebling U., Hernandez K., Heumann K.,
RA Hilger F., Hofmann B., Indge K.J., James C.M., Klima R., Koetter P.,
RA Kramer B., Kramer W., Lauquin G., Leuther H., Louis E.J., Maillier E.,
RA Marconi A., Martegani E., Mazon M.J., Mazzoni C., McReynolds A.D.K.,
RA Melchioretto P., Mewes H.-W., Minenkova O., Mueller-Auer S., Nawrocki A.,
RA Netter P., Neu R., Nombela C., Oliver S.G., Panzeri L., Paoluzi S.,
RA Plevani P., Portetelle D., Portillo F., Potier S., Purnelle B., Rieger M.,
RA Riles L., Rinaldi T., Robben J., Rodrigues-Pousada C.,
RA Rodriguez-Belmonte E., Rodriguez-Torres A.M., Rose M., Ruzzi M.,
RA Saliola M., Sanchez-Perez M., Schaefer B., Schaefer M., Scharfe M.,
RA Schmidheini T., Schreer A., Skala J., Souciet J.-L., Steensma H.Y.,
RA Talla E., Thierry A., Vandenbol M., van der Aart Q.J.M., Van Dyck L.,
RA Vanoni M., Verhasselt P., Voet M., Volckaert G., Wambutt R., Watson M.D.,
RA Weber N., Wedler E., Wedler H., Wipfli P., Wolf K., Wright L.F.,
RA Zaccaria P., Zimmermann M., Zollner A., Kleine K.;
RT "The nucleotide sequence of Saccharomyces cerevisiae chromosome VII.";
RL Nature 387:81-84(1997).
RN [3]
RP GENOME REANNOTATION.
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=24374639; DOI=10.1534/g3.113.008995;
RA Engel S.R., Dietrich F.S., Fisk D.G., Binkley G., Balakrishnan R.,
RA Costanzo M.C., Dwight S.S., Hitz B.C., Karra K., Nash R.S., Weng S.,
RA Wong E.D., Lloyd P., Skrzypek M.S., Miyasato S.R., Simison M., Cherry J.M.;
RT "The reference genome sequence of Saccharomyces cerevisiae: Then and now.";
RL G3 (Bethesda) 4:389-398(2014).
RN [4]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=17322287; DOI=10.1101/gr.6037607;
RA Hu Y., Rolfs A., Bhullar B., Murthy T.V.S., Zhu C., Berger M.F.,
RA Camargo A.A., Kelley F., McCarron S., Jepson D., Richardson A., Raphael J.,
RA Moreira D., Taycher E., Zuo D., Mohr S., Kane M.F., Williamson J.,
RA Simpson A.J.G., Bulyk M.L., Harlow E., Marsischky G., Kolodner R.D.,
RA LaBaer J.;
RT "Approaching a complete repository of sequence-verified protein-encoding
RT clones for Saccharomyces cerevisiae.";
RL Genome Res. 17:536-543(2007).
RN [5]
RP CHARACTERIZATION.
RX PubMed=1331085; DOI=10.1016/s0021-9258(18)50103-4;
RA Henry N.L., Sayre M.H., Kornberg R.D.;
RT "Purification and characterization of yeast RNA polymerase II general
RT initiation factor g.";
RL J. Biol. Chem. 267:23388-23392(1992).
RN [6]
RP LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
RX PubMed=14562106; DOI=10.1038/nature02046;
RA Ghaemmaghami S., Huh W.-K., Bower K., Howson R.W., Belle A., Dephoure N.,
RA O'Shea E.K., Weissman J.S.;
RT "Global analysis of protein expression in yeast.";
RL Nature 425:737-741(2003).
RN [7]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-56, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=18407956; DOI=10.1074/mcp.m700468-mcp200;
RA Albuquerque C.P., Smolka M.B., Payne S.H., Bafna V., Eng J., Zhou H.;
RT "A multidimensional chromatography technology for in-depth phosphoproteome
RT analysis.";
RL Mol. Cell. Proteomics 7:1389-1396(2008).
RN [8]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-28 AND SER-34, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=19779198; DOI=10.1126/science.1172867;
RA Holt L.J., Tuch B.B., Villen J., Johnson A.D., Gygi S.P., Morgan D.O.;
RT "Global analysis of Cdk1 substrate phosphorylation sites provides insights
RT into evolution.";
RL Science 325:1682-1686(2009).
CC -!- FUNCTION: TFIIF is a general transcription initiation factor that binds
CC to RNA polymerase II. Its functions include the recruitment of RNA
CC polymerase II to the promoter bound DNA-TBP-TFIIB complex, decreasing
CC the affinity of RNA polymerase II for non-specific DNA, allowing for
CC the subsequent recruitment of TFIIE and TFIIH, and facilitating RNA
CC polymerase II elongation. {ECO:0000250}.
CC -!- SUBUNIT: TFIIF is composed of three different subunits: TFG1/RAP74,
CC TFG2/RAP30 and TAF14.
CC -!- INTERACTION:
CC P41896; P38217: KAP104; NbExp=2; IntAct=EBI-18916, EBI-9152;
CC P41896; P08518: RPB2; NbExp=7; IntAct=EBI-18916, EBI-15767;
CC -!- SUBCELLULAR LOCATION: Nucleus.
CC -!- MISCELLANEOUS: Present with 520 molecules/cell in log phase SD medium.
CC {ECO:0000269|PubMed:14562106}.
CC -!- SIMILARITY: Belongs to the TFIIF beta subunit family. {ECO:0000305}.
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DR EMBL; U13016; AAA61642.1; -; Genomic_DNA.
DR EMBL; Z72790; CAA96988.1; -; Genomic_DNA.
DR EMBL; AY692871; AAT92890.1; -; Genomic_DNA.
DR EMBL; BK006941; DAA08103.1; -; Genomic_DNA.
DR PIR; S64294; S64294.
DR RefSeq; NP_011519.3; NM_001181134.3.
DR PDB; 4V1N; EM; 7.80 A; R=1-400.
DR PDB; 4V1O; EM; 9.70 A; R=1-400.
DR PDB; 5FMF; EM; 6.00 A; V=54-140, V=210-227, V=291-359.
DR PDB; 5FYW; EM; 4.35 A; R=1-400.
DR PDB; 5FZ5; EM; 8.80 A; R=1-400.
DR PDB; 5OQJ; EM; 4.70 A; R=1-400.
DR PDB; 5OQM; EM; 5.80 A; R=1-400.
DR PDB; 5SVA; EM; 15.30 A; g=1-400.
DR PDB; 6GYK; EM; 5.10 A; R=1-400.
DR PDB; 6GYL; EM; 4.80 A; R=1-400.
DR PDB; 6GYM; EM; 6.70 A; R=1-400.
DR PDB; 7O4I; EM; 3.20 A; R=1-400.
DR PDB; 7O4J; EM; 2.90 A; R=1-400.
DR PDB; 7O72; EM; 3.40 A; R=1-400.
DR PDB; 7O73; EM; 3.40 A; R=1-400.
DR PDB; 7O75; EM; 3.20 A; R=1-400.
DR PDBsum; 4V1N; -.
DR PDBsum; 4V1O; -.
DR PDBsum; 5FMF; -.
DR PDBsum; 5FYW; -.
DR PDBsum; 5FZ5; -.
DR PDBsum; 5OQJ; -.
DR PDBsum; 5OQM; -.
DR PDBsum; 5SVA; -.
DR PDBsum; 6GYK; -.
DR PDBsum; 6GYL; -.
DR PDBsum; 6GYM; -.
DR PDBsum; 7O4I; -.
DR PDBsum; 7O4J; -.
DR PDBsum; 7O72; -.
DR PDBsum; 7O73; -.
DR PDBsum; 7O75; -.
DR AlphaFoldDB; P41896; -.
DR BMRB; P41896; -.
DR SMR; P41896; -.
DR BioGRID; 33249; 253.
DR ComplexPortal; CPX-1149; Transcription factor TFIIF complex.
DR DIP; DIP-1152N; -.
DR IntAct; P41896; 32.
DR MINT; P41896; -.
DR STRING; 4932.YGR005C; -.
DR iPTMnet; P41896; -.
DR MaxQB; P41896; -.
DR PaxDb; P41896; -.
DR PRIDE; P41896; -.
DR EnsemblFungi; YGR005C_mRNA; YGR005C; YGR005C.
DR GeneID; 852888; -.
DR KEGG; sce:YGR005C; -.
DR SGD; S000003237; TFG2.
DR VEuPathDB; FungiDB:YGR005C; -.
DR eggNOG; KOG2905; Eukaryota.
DR GeneTree; ENSGT00390000016051; -.
DR HOGENOM; CLU_047858_0_1_1; -.
DR InParanoid; P41896; -.
DR OMA; ANCPEHQ; -.
DR BioCyc; YEAST:G3O-30736-MON; -.
DR Reactome; R-SCE-113418; Formation of the Early Elongation Complex.
DR Reactome; R-SCE-674695; RNA Polymerase II Pre-transcription Events.
DR Reactome; R-SCE-6796648; TP53 Regulates Transcription of DNA Repair Genes.
DR Reactome; R-SCE-6807505; RNA polymerase II transcribes snRNA genes.
DR Reactome; R-SCE-72086; mRNA Capping.
DR Reactome; R-SCE-73776; RNA Polymerase II Promoter Escape.
DR Reactome; R-SCE-73779; RNA Polymerase II Transcription Pre-Initiation And Promoter Opening.
DR Reactome; R-SCE-75953; RNA Polymerase II Transcription Initiation.
DR Reactome; R-SCE-75955; RNA Polymerase II Transcription Elongation.
DR Reactome; R-SCE-76042; RNA Polymerase II Transcription Initiation And Promoter Clearance.
DR Reactome; R-SCE-77075; RNA Pol II CTD phosphorylation and interaction with CE.
DR Reactome; R-SCE-9018519; Estrogen-dependent gene expression.
DR PRO; PR:P41896; -.
DR Proteomes; UP000002311; Chromosome VII.
DR RNAct; P41896; protein.
DR GO; GO:0005634; C:nucleus; IDA:ComplexPortal.
DR GO; GO:0005674; C:transcription factor TFIIF complex; IDA:SGD.
DR GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
DR GO; GO:0000166; F:nucleotide binding; IEA:UniProtKB-KW.
DR GO; GO:0000993; F:RNA polymerase II complex binding; IDA:SGD.
DR GO; GO:0001111; P:promoter clearance from RNA polymerase II promoter; IC:SGD.
DR GO; GO:0006355; P:regulation of transcription, DNA-templated; IDA:ComplexPortal.
DR GO; GO:0051123; P:RNA polymerase II preinitiation complex assembly; IPI:ComplexPortal.
DR GO; GO:0006368; P:transcription elongation from RNA polymerase II promoter; IDA:SGD.
DR GO; GO:0006367; P:transcription initiation from RNA polymerase II promoter; IDA:SGD.
DR GO; GO:0001174; P:transcriptional start site selection at RNA polymerase II promoter; IMP:SGD.
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 SUPFAM; SSF46785; SSF46785; 1.
DR SUPFAM; SSF50916; SSF50916; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Direct protein sequencing; DNA-binding; Nucleotide-binding;
KW Nucleus; Phosphoprotein; Reference proteome; Transcription;
KW Transcription regulation.
FT CHAIN 1..400
FT /note="Transcription initiation factor IIF subunit beta"
FT /id="PRO_0000211240"
FT REGION 1..47
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 165..194
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 366..400
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..31
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 385..400
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 28
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19779198"
FT MOD_RES 34
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19779198"
FT MOD_RES 56
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18407956"
FT CONFLICT 232
FT /note="N -> H (in Ref. 1; AAA61642)"
FT /evidence="ECO:0000305"
FT HELIX 49..52
FT /evidence="ECO:0007829|PDB:7O4J"
FT STRAND 60..63
FT /evidence="ECO:0007829|PDB:7O4I"
FT STRAND 67..72
FT /evidence="ECO:0007829|PDB:7O4J"
FT HELIX 75..81
FT /evidence="ECO:0007829|PDB:7O4J"
FT STRAND 91..98
FT /evidence="ECO:0007829|PDB:7O4J"
FT STRAND 104..108
FT /evidence="ECO:0007829|PDB:7O4J"
FT HELIX 110..112
FT /evidence="ECO:0007829|PDB:7O4J"
FT STRAND 114..116
FT /evidence="ECO:0007829|PDB:7O75"
FT STRAND 118..128
FT /evidence="ECO:0007829|PDB:7O4J"
FT STRAND 131..138
FT /evidence="ECO:0007829|PDB:7O4J"
FT STRAND 211..226
FT /evidence="ECO:0007829|PDB:7O4J"
FT TURN 231..234
FT /evidence="ECO:0007829|PDB:7O4J"
FT HELIX 235..245
FT /evidence="ECO:0007829|PDB:7O4J"
FT HELIX 259..262
FT /evidence="ECO:0007829|PDB:7O4J"
FT HELIX 263..265
FT /evidence="ECO:0007829|PDB:7O4J"
FT STRAND 266..268
FT /evidence="ECO:0007829|PDB:7O4J"
FT HELIX 280..285
FT /evidence="ECO:0007829|PDB:7O4J"
FT HELIX 296..309
FT /evidence="ECO:0007829|PDB:7O4J"
FT STRAND 311..313
FT /evidence="ECO:0007829|PDB:7O4I"
FT HELIX 315..322
FT /evidence="ECO:0007829|PDB:7O4J"
FT HELIX 326..336
FT /evidence="ECO:0007829|PDB:7O4J"
FT STRAND 337..345
FT /evidence="ECO:0007829|PDB:7O4J"
FT STRAND 348..351
FT /evidence="ECO:0007829|PDB:7O4J"
FT HELIX 353..356
FT /evidence="ECO:0007829|PDB:7O4J"
SQ SEQUENCE 400 AA; 46605 MW; DDDA895446BBF26F CRC64;
MSSGSAGAPA LSNNSTNSVA KEKSGNISGD EYLSQEEEVF DGNDIENNET KVYEESLDLD
LERSNRQVWL VRLPMFLAEK WRDRNNLHGQ ELGKIRINKD GSKITLLLNE NDNDSIPHEY
DLELTKKVVE NEYVFTEQNL KKYQQRKKEL EADPEKQRQA YLKKQEREEE LKKKQQQQKR
RNNRKKFNHR VMTDRDGRDR YIPYVKTIPK KTAIVGTVCH ECQVMPSMND PNYHKIVEQR
RNIVKLNNKE RITTLDETVG VTMSHTGMSM RSDNSNFLKV GREKAKSNIK SIRMPKKEIL
DYLFKLFDEY DYWSLKGLKE RTRQPEAHLK ECLDKVATLV KKGPYAFKYT LRPEYKKLKE
EERKATLGEL ADEQTGSAGD NAQGDAEADL EDEIEMEDVV
