ID   T2FA_MOUSE              Reviewed;         508 AA.
AC   Q3THK3; Q8R5B7;
DT   28-NOV-2006, integrated into UniProtKB/Swiss-Prot.
DT   27-JUL-2011, sequence version 2.
DT   27-MAR-2024, entry version 145.
DE   RecName: Full=General transcription factor IIF subunit 1;
DE   AltName: Full=Transcription initiation factor IIF subunit alpha;
DE            Short=TFIIF-alpha;
GN   Name=Gtf2f1;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC   Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=DBA/2J;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA   Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA   Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA   Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA   Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA   Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA   Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA   Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA   Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA   Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA   Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA   Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA   Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA   Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA   Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA   Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA   Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA   Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA   Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA   Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA   van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA   Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA   Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA   Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA   Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA   Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA   Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA   Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA   Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
RN   [2]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-221 AND SER-224, AND
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Teratocarcinoma;
RX   PubMed=17622165; DOI=10.1021/pr070122r;
RA   Smith J.C., Duchesne M.A., Tozzi P., Ethier M., Figeys D.;
RT   "A differential phosphoproteomic analysis of retinoic acid-treated P19
RT   cells.";
RL   J. Proteome Res. 6:3174-3186(2007).
RN   [3]
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Liver;
RX   PubMed=17242355; DOI=10.1073/pnas.0609836104;
RA   Villen J., Beausoleil S.A., Gerber S.A., Gygi S.P.;
RT   "Large-scale phosphorylation analysis of mouse liver.";
RL   Proc. Natl. Acad. Sci. U.S.A. 104:1488-1493(2007).
RN   [4]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-217; SER-218; SER-221;
RP   SER-224; THR-389 AND SER-433, AND IDENTIFICATION BY MASS SPECTROMETRY
RP   [LARGE SCALE ANALYSIS].
RC   TISSUE=Brain, Brown adipose tissue, Heart, Kidney, Liver, Lung,
RC   Pancreas, Spleen, and Testis;
RX   PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA   Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA   Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT   "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL   Cell 143:1174-1189(2010).
RN   [5]
RP   ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-407, AND IDENTIFICATION BY MASS
RP   SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Embryonic fibroblast;
RX   PubMed=23806337; DOI=10.1016/j.molcel.2013.06.001;
RA   Park J., Chen Y., Tishkoff D.X., Peng C., Tan M., Dai L., Xie Z., Zhang Y.,
RA   Zwaans B.M., Skinner M.E., Lombard D.B., Zhao Y.;
RT   "SIRT5-mediated lysine desuccinylation impacts diverse metabolic
RT   pathways.";
RL   Mol. Cell 50:919-930(2013).
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 (By
CC       similarity). {ECO:0000250}.
CC   -!- SUBUNIT: Heterodimer of an alpha and a beta subunit. Interacts with
CC       GTF2F2, CTDP1, TAF6/TAFII80 and URI1. Interacts with GTF2B (via C-
CC       terminus and preferentially via acetylated form); this interaction
CC       prevents binding of GTF2B to GTF2F2. Part of TBP-based Pol II pre-
CC       initiation complex (PIC), in which Pol II core assembles with general
CC       transcription factors and other specific initiation factors including
CC       GTF2E1, GTF2E2, GTF2F1, GTF2F2, TCEA1, ERCC2, ERCC3, GTF2H2, GTF2H3,
CC       GTF2H4, GTF2H5, GTF2A1, GTF2A2, GTF2B and TBP; this large multi-subunit
CC       PIC complex mediates DNA unwinding and targets Pol II core to the
CC       transcription start site where the first phosphodiester bond forms.
CC       {ECO:0000250|UniProtKB:P35269}.
CC   -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250}.
CC   -!- PTM: Phosphorylated on Ser and other residues by TAF1 and casein kinase
CC       II-like kinases. {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the TFIIF alpha subunit family. {ECO:0000305}.
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DR   EMBL; AK168236; BAE40186.1; -; mRNA.
DR   EMBL; AK168243; BAE40193.1; -; mRNA.
DR   EMBL; CH466537; EDL38221.1; -; Genomic_DNA.
DR   EMBL; BC023081; AAH23081.1; -; mRNA.
DR   EMBL; BC031123; AAH31123.1; -; mRNA.
DR   CCDS; CCDS37667.1; -.
DR   RefSeq; NP_598562.1; NM_133801.2.
DR   AlphaFoldDB; Q3THK3; -.
DR   SMR; Q3THK3; -.
DR   BioGRID; 220965; 32.
DR   ComplexPortal; CPX-83; General transcription factor TFIIF complex.
DR   CORUM; Q3THK3; -.
DR   IntAct; Q3THK3; 1.
DR   STRING; 10090.ENSMUSP00000002733; -.
DR   iPTMnet; Q3THK3; -.
DR   PhosphoSitePlus; Q3THK3; -.
DR   EPD; Q3THK3; -.
DR   jPOST; Q3THK3; -.
DR   MaxQB; Q3THK3; -.
DR   PaxDb; 10090-ENSMUSP00000002733; -.
DR   PeptideAtlas; Q3THK3; -.
DR   ProteomicsDB; 263053; -.
DR   Pumba; Q3THK3; -.
DR   Antibodypedia; 11855; 357 antibodies from 27 providers.
DR   DNASU; 98053; -.
DR   Ensembl; ENSMUST00000002733.7; ENSMUSP00000002733.7; ENSMUSG00000002658.10.
DR   GeneID; 98053; -.
DR   KEGG; mmu:98053; -.
DR   UCSC; uc008ddp.1; mouse.
DR   AGR; MGI:1923848; -.
DR   CTD; 2962; -.
DR   MGI; MGI:1923848; Gtf2f1.
DR   VEuPathDB; HostDB:ENSMUSG00000002658; -.
DR   eggNOG; KOG2393; Eukaryota.
DR   GeneTree; ENSGT00440000038032; -.
DR   HOGENOM; CLU_027572_2_0_1; -.
DR   InParanoid; Q3THK3; -.
DR   OMA; FATWHQA; -.
DR   OrthoDB; 2919205at2759; -.
DR   PhylomeDB; Q3THK3; -.
DR   TreeFam; TF313850; -.
DR   Reactome; R-MMU-112382; Formation of RNA Pol II elongation complex.
DR   Reactome; R-MMU-113418; Formation of the Early Elongation Complex.
DR   Reactome; R-MMU-674695; RNA Polymerase II Pre-transcription Events.
DR   Reactome; R-MMU-6796648; TP53 Regulates Transcription of DNA Repair Genes.
DR   Reactome; R-MMU-6803529; FGFR2 alternative splicing.
DR   Reactome; R-MMU-6807505; RNA polymerase II transcribes snRNA genes.
DR   Reactome; R-MMU-72086; mRNA Capping.
DR   Reactome; R-MMU-72163; mRNA Splicing - Major Pathway.
DR   Reactome; R-MMU-72165; mRNA Splicing - Minor Pathway.
DR   Reactome; R-MMU-72203; Processing of Capped Intron-Containing Pre-mRNA.
DR   Reactome; R-MMU-73776; RNA Polymerase II Promoter Escape.
DR   Reactome; R-MMU-73779; RNA Polymerase II Transcription Pre-Initiation And Promoter Opening.
DR   Reactome; R-MMU-75953; RNA Polymerase II Transcription Initiation.
DR   Reactome; R-MMU-75955; RNA Polymerase II Transcription Elongation.
DR   Reactome; R-MMU-76042; RNA Polymerase II Transcription Initiation And Promoter Clearance.
DR   Reactome; R-MMU-77075; RNA Pol II CTD phosphorylation and interaction with CE.
DR   Reactome; R-MMU-9018519; Estrogen-dependent gene expression.
DR   BioGRID-ORCS; 98053; 19 hits in 82 CRISPR screens.
DR   PRO; PR:Q3THK3; -.
DR   Proteomes; UP000000589; Chromosome 17.
DR   RNAct; Q3THK3; Protein.
DR   Bgee; ENSMUSG00000002658; Expressed in saccule of membranous labyrinth and 283 other cell types or tissues.
DR   GO; GO:0030054; C:cell junction; ISO:MGI.
DR   GO; GO:0043231; C:intracellular membrane-bounded organelle; ISO:MGI.
DR   GO; GO:0005654; C:nucleoplasm; ISO:MGI.
DR   GO; GO:0005634; C:nucleus; ISO:MGI.
DR   GO; GO:0032991; C:protein-containing complex; ISO:MGI.
DR   GO; GO:0005669; C:transcription factor TFIID complex; ISO:MGI.
DR   GO; GO:0005674; C:transcription factor TFIIF complex; ISO:MGI.
DR   GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
DR   GO; GO:0019211; F:phosphatase activator activity; ISO:MGI.
DR   GO; GO:1990841; F:promoter-specific chromatin binding; ISS:UniProtKB.
DR   GO; GO:0019904; F:protein domain specific binding; ISO:MGI.
DR   GO; GO:0019903; F:protein phosphatase binding; ISO:MGI.
DR   GO; GO:0016251; F:RNA polymerase II general transcription initiation factor activity; ISO:MGI.
DR   GO; GO:0001091; F:RNA polymerase II general transcription initiation factor binding; ISO:MGI.
DR   GO; GO:0001096; F:TFIIF-class transcription factor complex binding; IBA:GO_Central.
DR   GO; GO:0032091; P:negative regulation of protein binding; ISS:UniProtKB.
DR   GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; IDA:MGI.
DR   GO; GO:0032968; P:positive regulation of transcription elongation by RNA polymerase II; IEA:InterPro.
DR   GO; GO:0009615; P:response to virus; IEA:Ensembl.
DR   GO; GO:0006368; P:transcription elongation by RNA polymerase II; ISO:MGI.
DR   GO; GO:0006367; P:transcription initiation at RNA polymerase II promoter; ISO:MGI.
DR   CDD; cd00240; TFIIFa; 1.
DR   Gene3D; 1.10.10.10; Winged helix-like DNA-binding domain superfamily/Winged helix DNA-binding domain; 1.
DR   InterPro; IPR008851; TFIIF-alpha.
DR   InterPro; IPR011039; TFIIF_interaction.
DR   InterPro; IPR036388; WH-like_DNA-bd_sf.
DR   InterPro; IPR036390; WH_DNA-bd_sf.
DR   PANTHER; PTHR13011:SF0; GENERAL TRANSCRIPTION FACTOR IIF SUBUNIT 1; 1.
DR   PANTHER; PTHR13011; TFIIF-ALPHA; 1.
DR   Pfam; PF05793; TFIIF_alpha; 1.
DR   SUPFAM; SSF50916; Rap30/74 interaction domains; 2.
DR   SUPFAM; SSF46785; Winged helix' DNA-binding domain; 1.
DR   Genevisible; Q3THK3; MM.
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:P35269"
FT   CHAIN           2..508
FT                   /note="General transcription factor IIF subunit 1"
FT                   /id="PRO_0000260322"
FT   REGION          177..446
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        179..214
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        273..287
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        288..305
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        306..320
FT                   /note="Acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        321..345
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        380..413
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        429..444
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOD_RES         2
FT                   /note="N-acetylalanine"
FT                   /evidence="ECO:0000250|UniProtKB:P35269"
FT   MOD_RES         156
FT                   /note="Phosphothreonine"
FT                   /evidence="ECO:0000250|UniProtKB:P35269"
FT   MOD_RES         217
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:21183079"
FT   MOD_RES         218
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:21183079"
FT   MOD_RES         221
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:17622165,
FT                   ECO:0007744|PubMed:21183079"
FT   MOD_RES         224
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:17622165,
FT                   ECO:0007744|PubMed:21183079"
FT   MOD_RES         331
FT                   /note="Phosphothreonine"
FT                   /evidence="ECO:0000250|UniProtKB:P35269"
FT   MOD_RES         377
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:P35269"
FT   MOD_RES         380
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:P35269"
FT   MOD_RES         381
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:P35269"
FT   MOD_RES         385
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:P35269"
FT   MOD_RES         389
FT                   /note="Phosphothreonine"
FT                   /evidence="ECO:0007744|PubMed:21183079"
FT   MOD_RES         391
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:P35269"
FT   MOD_RES         407
FT                   /note="N6-acetyllysine"
FT                   /evidence="ECO:0007744|PubMed:23806337"
FT   MOD_RES         431
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:P35269"
FT   MOD_RES         433
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:21183079"
FT   MOD_RES         436
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:P35269"
FT   MOD_RES         437
FT                   /note="Phosphothreonine"
FT                   /evidence="ECO:0000250|UniProtKB:P35269"
FT   MOD_RES         440
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:P35269"
FT   CONFLICT        139
FT                   /note="P -> T (in Ref. 1; BAE40186/BAE40193)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        185
FT                   /note="Q -> E (in Ref. 1; BAE40186/BAE40193)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   508 AA;  57241 MW;  EB6DDD074CFBA712 CRC64;
     MAALGSSSQN VTEYVVRVPK NTAKRYNIMA FNAADKVNFA TWNQARLERD LSNKKIYQEE
     EMPESGAGSE FNRKLREEAR RKKYGIVLKE FRPEDQPWLL RVNGKSGRKF KGIKKGGVTE
     NTAYYIFTQC ADGAFEAFPV QNWYNFTPLA RHRTLTAEEA EEEWERRNKV LNHFSIMQQR
     RLKDQDQDED EEEKEKRSRK KPSELRIHDL EDDLEMSSDA SDASGEEGSR TSKAKKKAPV
     TKAGRKKKKK KGSDDEAFED SDDGDFEGQE VDYMSDGSSS SPDETEGKPK VPQQEDGPKG
     VDEQSESSEE SEEEKPPEED KEEEEEKKAP TPQEKKRRKD SSDDSDSSEE SDIDSETSSA
     LFMAKKKTPP KRERKPSGGS SKGTSRPGTP SAEAASTSST LRAAASKLEQ GKRTSETPAA
     KRLRMDTGPQ SLSGKSTPSS GDVQVTEDAV RRYLTRKPMT TKDLLKKFQT KKTGLSSEQT
     VNVLAQILKR LNPERKMIGD KMHFSLKE
//