T2FA_BOVIN
ID T2FA_BOVIN Reviewed; 517 AA.
AC Q5EA53; A6H7C0;
DT 28-NOV-2006, integrated into UniProtKB/Swiss-Prot.
DT 15-MAR-2005, sequence version 1.
DT 03-AUG-2022, entry version 115.
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 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].
RX PubMed=16305752; DOI=10.1186/1471-2164-6-166;
RA Harhay G.P., Sonstegard T.S., Keele J.W., Heaton M.P., Clawson M.L.,
RA Snelling W.M., Wiedmann R.T., Van Tassell C.P., Smith T.P.L.;
RT "Characterization of 954 bovine full-CDS cDNA sequences.";
RL BMC Genomics 6:166-166(2005).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=Hereford; TISSUE=Fetal skin;
RG NIH - Mammalian Gene Collection (MGC) project;
RL Submitted (JUN-2007) 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. 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 (By similarity). Interacts with
CC GTF2B (via C-terminus and preferentially via acetylated form); this
CC interaction prevents binding of GTF2B to GTF2F2 (By similarity).
CC {ECO:0000250, 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; BT020716; AAX08733.1; -; mRNA.
DR EMBL; BC146189; AAI46190.1; -; mRNA.
DR RefSeq; NP_001015527.1; NM_001015527.1.
DR AlphaFoldDB; Q5EA53; -.
DR SMR; Q5EA53; -.
DR STRING; 9913.ENSBTAP00000027988; -.
DR PaxDb; Q5EA53; -.
DR PRIDE; Q5EA53; -.
DR Ensembl; ENSBTAT00000027988; ENSBTAP00000027988; ENSBTAG00000021016.
DR GeneID; 505702; -.
DR KEGG; bta:505702; -.
DR CTD; 2962; -.
DR VEuPathDB; HostDB:ENSBTAG00000021016; -.
DR VGNC; VGNC:97277; GTF2F1.
DR eggNOG; KOG2393; Eukaryota.
DR GeneTree; ENSGT00440000038032; -.
DR HOGENOM; CLU_027572_2_0_1; -.
DR InParanoid; Q5EA53; -.
DR OMA; NNMKEFR; -.
DR OrthoDB; 893557at2759; -.
DR TreeFam; TF313850; -.
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 7.
DR Bgee; ENSBTAG00000021016; Expressed in retina and 109 other tissues.
DR GO; GO:0030054; C:cell junction; IEA:Ensembl.
DR GO; GO:0005669; C:transcription factor TFIID complex; IEA:Ensembl.
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:0019211; F:phosphatase activator activity; IEA:Ensembl.
DR GO; GO:1990841; F:promoter-specific chromatin binding; ISS:UniProtKB.
DR GO; GO:0019904; F:protein domain specific binding; IEA:Ensembl.
DR GO; GO:0019903; F:protein phosphatase binding; IEA:Ensembl.
DR GO; GO:0016251; F:RNA polymerase II general transcription initiation factor activity; IBA:GO_Central.
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; ISS:UniProtKB.
DR GO; GO:0032968; P:positive regulation of transcription elongation from RNA polymerase II promoter; IEA:InterPro.
DR GO; GO:0009615; P:response to virus; IEA:Ensembl.
DR GO; GO:0006368; P:transcription elongation from RNA polymerase II promoter; IEA:Ensembl.
DR GO; GO:0006367; P:transcription initiation from RNA polymerase II promoter; IBA:GO_Central.
DR Gene3D; 1.10.10.10; -; 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; PTHR13011; 1.
DR Pfam; PF05793; TFIIF_alpha; 1.
DR SUPFAM; SSF46785; SSF46785; 1.
DR SUPFAM; SSF50916; SSF50916; 2.
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:P35269"
FT CHAIN 2..517
FT /note="General transcription factor IIF subunit 1"
FT /id="PRO_0000260321"
FT REGION 178..458
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 179..213
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..453
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:0000250|UniProtKB:P35269"
FT MOD_RES 218
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P35269"
FT MOD_RES 221
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P35269"
FT MOD_RES 224
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P35269"
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:0000250|UniProtKB:P35269"
FT MOD_RES 391
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P35269"
FT MOD_RES 407
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:P35269"
FT MOD_RES 431
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P35269"
FT MOD_RES 433
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P35269"
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 446
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:P35269"
FT MOD_RES 449
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P35269"
SQ SEQUENCE 517 AA; 58262 MW; 9577D0BE30CBB3D8 CRC64;
MAALGPSSQN VTEYVVRVPK NTTKKYNIMA FNAADKVNLT TWNQARLERD LSNKKIYQEE
EMPESGAGSE FNRKLREEAR RKKYGIVLKE FRPEDQPWLL RVNGKSGRKF KGIKKGGVTE
NTSYYIFTQC PDGAFEAFPV HNWYNFTPLA KHRTLTAEEA EEEWERRNKV LNHFSIMQQR
RLKDQDQDEE DEEKEKRSRK KASELRIHDL EDDLEMSSDD SEASGEEGGR APKAKKKAPP
SKGGRKKKKK KGSDDEAFED SDDGDFEGQE VDYMSDGSSS SQDELEGKPK ATQQEEGPKG
VDEQSESSEE SEEEKPPEED KEEEEEKKAP TPQEKKRRKD SSEESDSSEE SDIDSEASSA
LFMAKKKTPP KRERKPSGGS SRGNSRPGTP STEAGSTSST LRAAASKLEQ GKRTSETPAA
KRLRLDTGPQ SLSGKSTPQP QSGKSTPSSG DVQVTEDAVR RYLTRKPMTT KDLLKKFQTK
KTGLSSEQTV NVLAQILKRL NPERKMINDK MHFSLKE
