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Q3THK3

- T2FA_MOUSE

UniProt

Q3THK3 - T2FA_MOUSE

Protein

General transcription factor IIF subunit 1

Gene

Gtf2f1

Organism
Mus musculus (Mouse)
Status
Reviewed - Annotation score: 4 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 85 (01 Oct 2014)
      Sequence version 2 (27 Jul 2011)
      Previous versions | rss
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    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

    1. catalytic activity Source: InterPro
    2. DNA binding Source: UniProtKB-KW
    3. phosphatase activator activity Source: Ensembl
    4. protein binding Source: MGI

    GO - Biological processi

    1. positive regulation of transcription from RNA polymerase II promoter Source: MGI
    2. response to virus Source: Ensembl
    3. transcription initiation from RNA polymerase II promoter Source: InterPro

    Keywords - Biological processi

    Transcription, Transcription regulation

    Keywords - Ligandi

    DNA-binding

    Enzyme and pathway databases

    ReactomeiREACT_203462. Formation of the Early Elongation Complex.
    REACT_226490. RNA Polymerase II Transcription Elongation.

    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: Chromosome 17

    Organism-specific databases

    MGIiMGI:1923848. Gtf2f1.

    Subcellular locationi

    Nucleus By similarity

    GO - Cellular componenti

    1. cell junction Source: Ensembl
    2. nucleus Source: UniProtKB-SubCell

    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.
    GenevestigatoriQ3THK3.

    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.

    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.
    InParanoidiQ8R5B7.
    KOiK03138.
    OMAiEMPAAKR.
    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

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    MAALGSSSQN VTEYVVRVPK NTAKRYNIMA FNAADKVNFA TWNQARLERD    50
    LSNKKIYQEE EMPESGAGSE FNRKLREEAR RKKYGIVLKE FRPEDQPWLL 100
    RVNGKSGRKF KGIKKGGVTE NTAYYIFTQC ADGAFEAFPV QNWYNFTPLA 150
    RHRTLTAEEA EEEWERRNKV LNHFSIMQQR RLKDQDQDED EEEKEKRSRK 200
    KPSELRIHDL EDDLEMSSDA SDASGEEGSR TSKAKKKAPV TKAGRKKKKK 250
    KGSDDEAFED SDDGDFEGQE VDYMSDGSSS SPDETEGKPK VPQQEDGPKG 300
    VDEQSESSEE SEEEKPPEED KEEEEEKKAP TPQEKKRRKD SSDDSDSSEE 350
    SDIDSETSSA LFMAKKKTPP KRERKPSGGS SKGTSRPGTP SAEAASTSST 400
    LRAAASKLEQ GKRTSETPAA KRLRMDTGPQ SLSGKSTPSS GDVQVTEDAV 450
    RRYLTRKPMT TKDLLKKFQT KKTGLSSEQT VNVLAQILKR LNPERKMIGD 500
    KMHFSLKE 508
    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:
    EMBL
    GenBank
    DDBJ
    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:
    EMBL
    GenBank
    DDBJ
    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 .
    CCDSi CCDS37667.1.
    RefSeqi NP_598562.1. NM_133801.2.
    UniGenei Mm.24632.

    3D structure databases

    ProteinModelPortali Q3THK3.
    SMRi Q3THK3. Positions 7-168, 440-508.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 220965. 2 interactions.
    IntActi Q3THK3. 1 interaction.
    MINTi MINT-4119252.

    PTM databases

    PhosphoSitei Q3THK3.

    Proteomic databases

    MaxQBi Q3THK3.
    PaxDbi Q3THK3.
    PRIDEi Q3THK3.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENSMUST00000002733 ; ENSMUSP00000002733 ; ENSMUSG00000002658 .
    GeneIDi 98053.
    KEGGi mmu:98053.
    UCSCi uc008ddp.1. mouse.

    Organism-specific databases

    CTDi 2962.
    MGIi MGI:1923848. Gtf2f1.

    Phylogenomic databases

    eggNOGi NOG244830.
    GeneTreei ENSGT00440000038032.
    HOGENOMi HOG000059644.
    HOVERGENi HBG000729.
    InParanoidi Q8R5B7.
    KOi K03138.
    OMAi EMPAAKR.
    OrthoDBi EOG7GXPBV.
    TreeFami TF313850.

    Enzyme and pathway databases

    Reactomei REACT_203462. Formation of the Early Elongation Complex.
    REACT_226490. RNA Polymerase II Transcription Elongation.

    Miscellaneous databases

    NextBioi 353268.
    PROi Q3THK3.
    SOURCEi Search...

    Gene expression databases

    Bgeei Q3THK3.
    CleanExi MM_GTF2F1.
    Genevestigatori Q3THK3.

    Family and domain databases

    Gene3Di 1.10.10.10. 1 hit.
    InterProi IPR008851. TFIIF-alpha.
    IPR011039. TFIIF_interaction.
    IPR011991. WHTH_DNA-bd_dom.
    [Graphical view ]
    Pfami PF05793. TFIIF_alpha. 1 hit.
    [Graphical view ]
    SUPFAMi SSF50916. SSF50916. 2 hits.
    ProtoNeti Search...

    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: October 1, 2014
    This is version 85 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