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Protein

General transcription factor IIF subunit 1

Gene

Gtf2f1

Organism
Mus musculus (Mouse)
Status
Reviewed-Annotation score: Annotation score: 4 out of 5-Experimental evidence at protein leveli

Functioni

TFIIF is a general transcription initiation factor that binds to RNA polymerase II and helps to recruit it to the initiation complex in collaboration with TFIIB. It promotes transcription elongation (By similarity).By similarity

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Biological processi

Transcription, Transcription regulation

Keywords - Ligandi

DNA-binding

Enzyme and pathway databases

ReactomeiREACT_271571. mRNA Splicing - Minor Pathway.
REACT_282911. RNA Polymerase II Pre-transcription Events.
REACT_283211. RNA Polymerase II Transcription Pre-Initiation And Promoter Opening.
REACT_296420. RNA Pol II CTD phosphorylation and interaction with CE.
REACT_307866. mRNA Splicing - Major Pathway.
REACT_308057. Formation of the Early Elongation Complex.
REACT_315215. RNA Polymerase II Transcription Elongation.
REACT_326102. Formation of RNA Pol II elongation complex.
REACT_329615. RNA Polymerase II Transcription Initiation And Promoter Clearance.
REACT_338828. mRNA Capping.
REACT_340895. Processing of Capped Intron-Containing Pre-mRNA.
REACT_342690. RNA Polymerase II Transcription Initiation.
REACT_349121. RNA Polymerase II Promoter Escape.

Names & Taxonomyi

Protein namesi
Recommended name:
General transcription factor IIF subunit 1
Alternative name(s):
Transcription initiation factor IIF subunit alpha
Short name:
TFIIF-alpha
Gene namesi
Name:Gtf2f1
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
ProteomesiUP000000589 Componenti: Chromosome 17

Organism-specific databases

MGIiMGI:1923848. Gtf2f1.

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Nucleus

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methioninei1 – 11RemovedBy similarity
Chaini2 – 508507General transcription factor IIF subunit 1PRO_0000260322Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei2 – 21N-acetylalanineBy similarity
Modified residuei217 – 2171PhosphoserineBy similarity
Modified residuei218 – 2181PhosphoserineBy similarity
Modified residuei221 – 2211Phosphoserine1 Publication
Modified residuei224 – 2241Phosphoserine1 Publication
Modified residuei331 – 3311PhosphothreonineBy similarity
Modified residuei377 – 3771PhosphoserineBy similarity
Modified residuei380 – 3801PhosphoserineBy similarity
Modified residuei381 – 3811PhosphoserineBy similarity
Modified residuei385 – 3851PhosphoserineBy similarity
Modified residuei389 – 3891PhosphothreonineBy similarity
Modified residuei391 – 3911PhosphoserineBy similarity
Modified residuei407 – 4071N6-acetyllysine1 Publication
Modified residuei431 – 4311PhosphoserineBy similarity
Modified residuei433 – 4331PhosphoserineBy similarity
Modified residuei436 – 4361PhosphoserineBy similarity
Modified residuei437 – 4371PhosphothreonineBy similarity
Modified residuei440 – 4401PhosphoserineBy similarity

Post-translational modificationi

Phosphorylated on Ser and other residues by TAF1 and casein kinase II-like kinases.By similarity

Keywords - PTMi

Acetylation, Phosphoprotein

Proteomic databases

MaxQBiQ3THK3.
PaxDbiQ3THK3.
PRIDEiQ3THK3.

PTM databases

PhosphoSiteiQ3THK3.

Expressioni

Gene expression databases

BgeeiQ3THK3.
CleanExiMM_GTF2F1.
GenevisibleiQ3THK3. MM.

Interactioni

Subunit structurei

Heterodimer of an alpha and a beta subunit. Interacts with GTF2F2, CTDP1, TAF6/TAFII80 and URI1 (By similarity).By similarity

Protein-protein interaction databases

BioGridi220965. 2 interactions.
IntActiQ3THK3. 1 interaction.
MINTiMINT-4119252.
STRINGi10090.ENSMUSP00000002733.

Structurei

3D structure databases

ProteinModelPortaliQ3THK3.
SMRiQ3THK3. Positions 7-168, 440-508.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Compositional bias

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Compositional biasi283 – 35068Glu-richAdd
BLAST

Sequence similaritiesi

Belongs to the TFIIF alpha subunit family.Curated

Phylogenomic databases

eggNOGiNOG244830.
GeneTreeiENSGT00440000038032.
HOGENOMiHOG000059644.
HOVERGENiHBG000729.
InParanoidiQ3THK3.
KOiK03138.
OMAiNINDKMH.
OrthoDBiEOG7GXPBV.
TreeFamiTF313850.

Family and domain databases

Gene3Di1.10.10.10. 1 hit.
InterProiIPR008851. TFIIF-alpha.
IPR011039. TFIIF_interaction.
IPR011991. WHTH_DNA-bd_dom.
[Graphical view]
PfamiPF05793. TFIIF_alpha. 1 hit.
[Graphical view]
SUPFAMiSSF50916. SSF50916. 2 hits.

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

Q3THK3-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MAALGSSSQN VTEYVVRVPK NTAKRYNIMA FNAADKVNFA TWNQARLERD
60 70 80 90 100
LSNKKIYQEE EMPESGAGSE FNRKLREEAR RKKYGIVLKE FRPEDQPWLL
110 120 130 140 150
RVNGKSGRKF KGIKKGGVTE NTAYYIFTQC ADGAFEAFPV QNWYNFTPLA
160 170 180 190 200
RHRTLTAEEA EEEWERRNKV LNHFSIMQQR RLKDQDQDED EEEKEKRSRK
210 220 230 240 250
KPSELRIHDL EDDLEMSSDA SDASGEEGSR TSKAKKKAPV TKAGRKKKKK
260 270 280 290 300
KGSDDEAFED SDDGDFEGQE VDYMSDGSSS SPDETEGKPK VPQQEDGPKG
310 320 330 340 350
VDEQSESSEE SEEEKPPEED KEEEEEKKAP TPQEKKRRKD SSDDSDSSEE
360 370 380 390 400
SDIDSETSSA LFMAKKKTPP KRERKPSGGS SKGTSRPGTP SAEAASTSST
410 420 430 440 450
LRAAASKLEQ GKRTSETPAA KRLRMDTGPQ SLSGKSTPSS GDVQVTEDAV
460 470 480 490 500
RRYLTRKPMT TKDLLKKFQT KKTGLSSEQT VNVLAQILKR LNPERKMIGD

KMHFSLKE
Length:508
Mass (Da):57,241
Last modified:July 27, 2011 - v2
Checksum:iEB6DDD074CFBA712
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti139 – 1391P → T in BAE40186 (PubMed:16141072).Curated
Sequence conflicti139 – 1391P → T in BAE40193 (PubMed:16141072).Curated
Sequence conflicti185 – 1851Q → E in BAE40186 (PubMed:16141072).Curated
Sequence conflicti185 – 1851Q → E in BAE40193 (PubMed:16141072).Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AK168236 mRNA. Translation: BAE40186.1.
AK168243 mRNA. Translation: BAE40193.1.
CH466537 Genomic DNA. Translation: EDL38221.1.
BC023081 mRNA. Translation: AAH23081.1.
BC031123 mRNA. Translation: AAH31123.1.
CCDSiCCDS37667.1.
RefSeqiNP_598562.1. NM_133801.2.
UniGeneiMm.24632.

Genome annotation databases

EnsembliENSMUST00000002733; ENSMUSP00000002733; ENSMUSG00000002658.
GeneIDi98053.
KEGGimmu:98053.
UCSCiuc008ddp.1. mouse.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AK168236 mRNA. Translation: BAE40186.1.
AK168243 mRNA. Translation: BAE40193.1.
CH466537 Genomic DNA. Translation: EDL38221.1.
BC023081 mRNA. Translation: AAH23081.1.
BC031123 mRNA. Translation: AAH31123.1.
CCDSiCCDS37667.1.
RefSeqiNP_598562.1. NM_133801.2.
UniGeneiMm.24632.

3D structure databases

ProteinModelPortaliQ3THK3.
SMRiQ3THK3. Positions 7-168, 440-508.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi220965. 2 interactions.
IntActiQ3THK3. 1 interaction.
MINTiMINT-4119252.
STRINGi10090.ENSMUSP00000002733.

PTM databases

PhosphoSiteiQ3THK3.

Proteomic databases

MaxQBiQ3THK3.
PaxDbiQ3THK3.
PRIDEiQ3THK3.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSMUST00000002733; ENSMUSP00000002733; ENSMUSG00000002658.
GeneIDi98053.
KEGGimmu:98053.
UCSCiuc008ddp.1. mouse.

Organism-specific databases

CTDi2962.
MGIiMGI:1923848. Gtf2f1.

Phylogenomic databases

eggNOGiNOG244830.
GeneTreeiENSGT00440000038032.
HOGENOMiHOG000059644.
HOVERGENiHBG000729.
InParanoidiQ3THK3.
KOiK03138.
OMAiNINDKMH.
OrthoDBiEOG7GXPBV.
TreeFamiTF313850.

Enzyme and pathway databases

ReactomeiREACT_271571. mRNA Splicing - Minor Pathway.
REACT_282911. RNA Polymerase II Pre-transcription Events.
REACT_283211. RNA Polymerase II Transcription Pre-Initiation And Promoter Opening.
REACT_296420. RNA Pol II CTD phosphorylation and interaction with CE.
REACT_307866. mRNA Splicing - Major Pathway.
REACT_308057. Formation of the Early Elongation Complex.
REACT_315215. RNA Polymerase II Transcription Elongation.
REACT_326102. Formation of RNA Pol II elongation complex.
REACT_329615. RNA Polymerase II Transcription Initiation And Promoter Clearance.
REACT_338828. mRNA Capping.
REACT_340895. Processing of Capped Intron-Containing Pre-mRNA.
REACT_342690. RNA Polymerase II Transcription Initiation.
REACT_349121. RNA Polymerase II Promoter Escape.

Miscellaneous databases

NextBioi353268.
PROiQ3THK3.
SOURCEiSearch...

Gene expression databases

BgeeiQ3THK3.
CleanExiMM_GTF2F1.
GenevisibleiQ3THK3. MM.

Family and domain databases

Gene3Di1.10.10.10. 1 hit.
InterProiIPR008851. TFIIF-alpha.
IPR011039. TFIIF_interaction.
IPR011991. WHTH_DNA-bd_dom.
[Graphical view]
PfamiPF05793. TFIIF_alpha. 1 hit.
[Graphical view]
SUPFAMiSSF50916. SSF50916. 2 hits.
ProtoNetiSearch...

Publicationsi

  1. "The transcriptional landscape of the mammalian genome."
    Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.
    , Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.
    Science 309:1559-1563(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Strain: DBA/2.
  2. "A differential phosphoproteomic analysis of retinoic acid-treated P19 cells."
    Smith J.C., Duchesne M.A., Tozzi P., Ethier M., Figeys D.
    J. Proteome Res. 6:3174-3186(2007) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-221 AND SER-224, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Teratocarcinoma.
  3. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Liver.
  4. "SIRT5-mediated lysine desuccinylation impacts diverse metabolic pathways."
    Park J., Chen Y., Tishkoff D.X., Peng C., Tan M., Dai L., Xie Z., Zhang Y., Zwaans B.M., Skinner M.E., Lombard D.B., Zhao Y.
    Mol. Cell 50:919-930(2013) [PubMed] [Europe PMC] [Abstract]
    Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-407, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Embryonic fibroblast.

Entry informationi

Entry nameiT2FA_MOUSE
AccessioniPrimary (citable) accession number: Q3THK3
Secondary accession number(s): Q8R5B7
Entry historyi
Integrated into UniProtKB/Swiss-Prot: November 28, 2006
Last sequence update: July 27, 2011
Last modified: June 24, 2015
This is version 92 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. MGD cross-references
    Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
  2. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.