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P35269

- T2FA_HUMAN

UniProt

P35269 - T2FA_HUMAN

Protein

General transcription factor IIF subunit 1

Gene

GTF2F1

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 153 (01 Oct 2014)
      Sequence version 2 (13 Apr 2004)
      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.1 Publication

    GO - Molecular functioni

    1. catalytic activity Source: InterPro
    2. DNA binding Source: UniProtKB-KW
    3. phosphatase activator activity Source: UniProtKB
    4. poly(A) RNA binding Source: UniProtKB
    5. protein binding Source: UniProtKB
    6. transcription coactivator activity Source: ProtInc
    7. transcription factor binding Source: BHF-UCL

    GO - Biological processi

    1. 7-methylguanosine mRNA capping Source: Reactome
    2. gene expression Source: Reactome
    3. mRNA splicing, via spliceosome Source: Reactome
    4. positive regulation of catalytic activity Source: GOC
    5. positive regulation of transcription from RNA polymerase II promoter Source: Ensembl
    6. positive regulation of viral transcription Source: Reactome
    7. response to virus Source: UniProtKB
    8. RNA splicing Source: Reactome
    9. transcription elongation from RNA polymerase II promoter Source: Reactome
    10. transcription from RNA polymerase II promoter Source: Reactome
    11. transcription initiation from RNA polymerase II promoter Source: Reactome
    12. viral process Source: Reactome

    Keywords - Biological processi

    Transcription, Transcription regulation

    Keywords - Ligandi

    DNA-binding

    Enzyme and pathway databases

    ReactomeiREACT_125. Processing of Capped Intron-Containing Pre-mRNA.
    REACT_1470. mRNA Capping.
    REACT_1655. RNA Polymerase II Transcription Pre-Initiation And Promoter Opening.
    REACT_1753. mRNA Splicing - Minor Pathway.
    REACT_1851. RNA Polymerase II Transcription Initiation.
    REACT_2089. RNA Polymerase II Promoter Escape.
    REACT_22107. RNA Polymerase II Pre-transcription Events.
    REACT_22201. Formation of HIV elongation complex in the absence of HIV Tat.
    REACT_467. mRNA Splicing - Major Pathway.
    REACT_6143. Pausing and recovery of Tat-mediated HIV elongation.
    REACT_6162. Tat-mediated elongation of the HIV-1 transcript.
    REACT_6233. Transcription of the HIV genome.
    REACT_6237. RNA Pol II CTD phosphorylation and interaction with CE.
    REACT_6244. Pausing and recovery of HIV elongation.
    REACT_6253. RNA Polymerase II HIV Promoter Escape.
    REACT_6259. HIV elongation arrest and recovery.
    REACT_6261. Abortive elongation of HIV-1 transcript in the absence of Tat.
    REACT_6319. Formation of the HIV-1 Early Elongation Complex.
    REACT_6332. HIV Transcription Initiation.
    REACT_6344. Tat-mediated HIV elongation arrest and recovery.
    REACT_6346. Formation of HIV-1 elongation complex containing HIV-1 Tat.
    REACT_6354. Viral Messenger RNA Synthesis.
    REACT_833. RNA Polymerase II Transcription Elongation.
    REACT_834. RNA Polymerase II Transcription Initiation And Promoter Clearance.
    REACT_846. Formation of the Early Elongation Complex.
    REACT_975. RNA Pol II CTD phosphorylation and interaction with CE.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    General transcription factor IIF subunit 1
    Alternative name(s):
    General transcription factor IIF 74 kDa subunit
    Transcription initiation factor IIF subunit alpha
    Short name:
    TFIIF-alpha
    Transcription initiation factor RAP74
    Gene namesi
    Name:GTF2F1
    Synonyms:RAP74
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 19

    Organism-specific databases

    HGNCiHGNC:4652. GTF2F1.

    Subcellular locationi

    GO - Cellular componenti

    1. cell junction Source: HPA
    2. nucleoplasm Source: Reactome
    3. nucleus Source: HPA
    4. transcription factor TFIIF complex Source: ProtInc

    Keywords - Cellular componenti

    Nucleus

    Pathology & Biotechi

    Mutagenesis

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Mutagenesisi385 – 3851S → A: Eliminates putative kinase activity; when associated with A-389. 1 Publication
    Mutagenesisi389 – 3891T → A: Eliminates putative kinase activity; when associated with A-385. 1 Publication

    Organism-specific databases

    PharmGKBiPA29038.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Initiator methioninei1 – 11Removed3 Publications
    Chaini2 – 517516General transcription factor IIF subunit 1PRO_0000211231Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei2 – 21N-acetylalanine3 Publications
    Modified residuei217 – 2171Phosphoserine5 Publications
    Modified residuei218 – 2181Phosphoserine5 Publications
    Modified residuei221 – 2211Phosphoserine4 Publications
    Modified residuei224 – 2241Phosphoserine5 Publications
    Modified residuei331 – 3311Phosphothreonine2 Publications
    Modified residuei377 – 3771Phosphoserine2 Publications
    Modified residuei380 – 3801Phosphoserine2 Publications
    Modified residuei381 – 3811Phosphoserine2 Publications
    Modified residuei385 – 3851Phosphoserine5 Publications
    Modified residuei389 – 3891Phosphothreonine4 Publications
    Modified residuei391 – 3911Phosphoserine2 Publications
    Modified residuei407 – 4071N6-acetyllysine1 Publication
    Modified residuei431 – 4311Phosphoserine2 Publications
    Modified residuei433 – 4331Phosphoserine4 Publications
    Modified residuei436 – 4361Phosphoserine2 Publications
    Modified residuei446 – 4461Phosphothreonine2 Publications
    Modified residuei449 – 4491Phosphoserine2 Publications

    Post-translational modificationi

    Phosphorylated on Ser and other residues by TAF1 and casein kinase II-like kinases.8 Publications

    Keywords - PTMi

    Acetylation, Phosphoprotein

    Proteomic databases

    MaxQBiP35269.
    PaxDbiP35269.
    PeptideAtlasiP35269.
    PRIDEiP35269.

    PTM databases

    PhosphoSiteiP35269.

    Miscellaneous databases

    PMAP-CutDBP35269.

    Expressioni

    Inductioni

    Up-regulated in response to enterovirus 71 (EV71) infection.1 Publication

    Gene expression databases

    ArrayExpressiP35269.
    BgeeiP35269.
    CleanExiHS_GTF2F1.
    GenevestigatoriP35269.

    Organism-specific databases

    HPAiHPA022793.

    Interactioni

    Subunit structurei

    Heterodimer of an alpha and a beta subunit. Interacts with GTF2F2, CTDP1, TAF6/TAFII80 and URI1.4 Publications

    Binary interactionsi

    WithEntry#Exp.IntActNotes
    TAF1P216753EBI-457886,EBI-491289
    URI1O947633EBI-457886,EBI-357067

    Protein-protein interaction databases

    BioGridi109217. 64 interactions.
    DIPiDIP-677N.
    IntActiP35269. 11 interactions.
    MINTiMINT-1403790.
    STRINGi9606.ENSP00000377969.

    Structurei

    Secondary structure

    1
    517
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Beta strandi10 – 178
    Beta strandi23 – 319
    Helixi33 – 353
    Helixi39 – 413
    Beta strandi45 – 495
    Helixi52 – 554
    Beta strandi58 – 614
    Helixi76 – 783
    Beta strandi84 – 874
    Beta strandi98 – 1047
    Beta strandi109 – 1146
    Beta strandi120 – 12910
    Beta strandi135 – 14814
    Helixi149 – 1513
    Helixi456 – 46510
    Helixi470 – 4756
    Helixi479 – 4824
    Helixi486 – 50015
    Beta strandi503 – 5075
    Beta strandi510 – 5156

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    1F3UX-ray1.70B/D/F/H2-172[»]
    1I27X-ray1.02A449-517[»]
    1J2XX-ray2.00A449-517[»]
    1NHANMR-A436-517[»]
    1ONVNMR-A436-517[»]
    2K7LNMR-A451-517[»]
    ProteinModelPortaliP35269.
    SMRiP35269. Positions 7-168, 449-517.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiP35269.

    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.
    HOGENOMiHOG000059644.
    HOVERGENiHBG000729.
    InParanoidiP35269.
    KOiK03138.
    OMAiEMPAAKR.
    OrthoDBiEOG7GXPBV.
    PhylomeDBiP35269.
    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.

    P35269-1 [UniParc]FASTAAdd to Basket

    « Hide

    MAALGPSSQN VTEYVVRVPK NTTKKYNIMA FNAADKVNFA TWNQARLERD    50
    LSNKKIYQEE EMPESGAGSE FNRKLREEAR RKKYGIVLKE FRPEDQPWLL 100
    RVNGKSGRKF KGIKKGGVTE NTSYYIFTQC PDGAFEAFPV HNWYNFTPLA 150
    RHRTLTAEEA EEEWERRNKV LNHFSIMQQR RLKDQDQDED EEEKEKRGRR 200
    KASELRIHDL EDDLEMSSDA SDASGEEGGR VPKAKKKAPL AKGGRKKKKK 250
    KGSDDEAFED SDDGDFEGQE VDYMSDGSSS SQEEPESKAK APQQEEGPKG 300
    VDEQSDSSEE SEEEKPPEED KEEEEEKKAP TPQEKKRRKD SSEESDSSEE 350
    SDIDSEASSA LFMAKKKTPP KRERKPSGGS SRGNSRPGTP SAEGGSTSST 400
    LRAAASKLEQ GKRVSEMPAA KRLRLDTGPQ SLSGKSTPQP PSGKTTPNSG 450
    DVQVTEDAVR RYLTRKPMTT KDLLKKFQTK KTGLSSEQTV NVLAQILKRL 500
    NPERKMINDK MHFSLKE 517
    Length:517
    Mass (Da):58,240
    Last modified:April 13, 2004 - v2
    Checksum:i1032B04A36BDC24F
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti231 – 2311V → I in CAA45404. (PubMed:1734284)Curated
    Sequence conflicti361 – 3611L → F in CAA45408. (PubMed:1734283)Curated

    Natural variant

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti3 – 31A → V.
    Corresponds to variant rs34826931 [ dbSNP | Ensembl ].
    VAR_039004

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    X64037 mRNA. Translation: CAA45408.1.
    X64002 mRNA. Translation: CAA45404.1.
    BT007097 mRNA. Translation: AAP35761.1.
    AK315240 mRNA. Translation: BAG37667.1.
    CH471139 Genomic DNA. Translation: EAW69098.1.
    BC000120 mRNA. Translation: AAH00120.1.
    BC013007 mRNA. Translation: AAH13007.1.
    CCDSiCCDS12165.1.
    PIRiS20248.
    RefSeqiNP_002087.2. NM_002096.2.
    UniGeneiHs.68257.

    Genome annotation databases

    EnsembliENST00000394456; ENSP00000377969; ENSG00000125651.
    GeneIDi2962.
    KEGGihsa:2962.
    UCSCiuc002meq.2. human.

    Polymorphism databases

    DMDMi46397744.

    Keywords - Coding sequence diversityi

    Polymorphism

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    X64037 mRNA. Translation: CAA45408.1 .
    X64002 mRNA. Translation: CAA45404.1 .
    BT007097 mRNA. Translation: AAP35761.1 .
    AK315240 mRNA. Translation: BAG37667.1 .
    CH471139 Genomic DNA. Translation: EAW69098.1 .
    BC000120 mRNA. Translation: AAH00120.1 .
    BC013007 mRNA. Translation: AAH13007.1 .
    CCDSi CCDS12165.1.
    PIRi S20248.
    RefSeqi NP_002087.2. NM_002096.2.
    UniGenei Hs.68257.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    1F3U X-ray 1.70 B/D/F/H 2-172 [» ]
    1I27 X-ray 1.02 A 449-517 [» ]
    1J2X X-ray 2.00 A 449-517 [» ]
    1NHA NMR - A 436-517 [» ]
    1ONV NMR - A 436-517 [» ]
    2K7L NMR - A 451-517 [» ]
    ProteinModelPortali P35269.
    SMRi P35269. Positions 7-168, 449-517.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 109217. 64 interactions.
    DIPi DIP-677N.
    IntActi P35269. 11 interactions.
    MINTi MINT-1403790.
    STRINGi 9606.ENSP00000377969.

    PTM databases

    PhosphoSitei P35269.

    Polymorphism databases

    DMDMi 46397744.

    Proteomic databases

    MaxQBi P35269.
    PaxDbi P35269.
    PeptideAtlasi P35269.
    PRIDEi P35269.

    Protocols and materials databases

    DNASUi 2962.
    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000394456 ; ENSP00000377969 ; ENSG00000125651 .
    GeneIDi 2962.
    KEGGi hsa:2962.
    UCSCi uc002meq.2. human.

    Organism-specific databases

    CTDi 2962.
    GeneCardsi GC19M006381.
    HGNCi HGNC:4652. GTF2F1.
    HPAi HPA022793.
    MIMi 189968. gene.
    neXtProti NX_P35269.
    PharmGKBi PA29038.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi NOG244830.
    HOGENOMi HOG000059644.
    HOVERGENi HBG000729.
    InParanoidi P35269.
    KOi K03138.
    OMAi EMPAAKR.
    OrthoDBi EOG7GXPBV.
    PhylomeDBi P35269.
    TreeFami TF313850.

    Enzyme and pathway databases

    Reactomei REACT_125. Processing of Capped Intron-Containing Pre-mRNA.
    REACT_1470. mRNA Capping.
    REACT_1655. RNA Polymerase II Transcription Pre-Initiation And Promoter Opening.
    REACT_1753. mRNA Splicing - Minor Pathway.
    REACT_1851. RNA Polymerase II Transcription Initiation.
    REACT_2089. RNA Polymerase II Promoter Escape.
    REACT_22107. RNA Polymerase II Pre-transcription Events.
    REACT_22201. Formation of HIV elongation complex in the absence of HIV Tat.
    REACT_467. mRNA Splicing - Major Pathway.
    REACT_6143. Pausing and recovery of Tat-mediated HIV elongation.
    REACT_6162. Tat-mediated elongation of the HIV-1 transcript.
    REACT_6233. Transcription of the HIV genome.
    REACT_6237. RNA Pol II CTD phosphorylation and interaction with CE.
    REACT_6244. Pausing and recovery of HIV elongation.
    REACT_6253. RNA Polymerase II HIV Promoter Escape.
    REACT_6259. HIV elongation arrest and recovery.
    REACT_6261. Abortive elongation of HIV-1 transcript in the absence of Tat.
    REACT_6319. Formation of the HIV-1 Early Elongation Complex.
    REACT_6332. HIV Transcription Initiation.
    REACT_6344. Tat-mediated HIV elongation arrest and recovery.
    REACT_6346. Formation of HIV-1 elongation complex containing HIV-1 Tat.
    REACT_6354. Viral Messenger RNA Synthesis.
    REACT_833. RNA Polymerase II Transcription Elongation.
    REACT_834. RNA Polymerase II Transcription Initiation And Promoter Clearance.
    REACT_846. Formation of the Early Elongation Complex.
    REACT_975. RNA Pol II CTD phosphorylation and interaction with CE.

    Miscellaneous databases

    ChiTaRSi GTF2F1. human.
    EvolutionaryTracei P35269.
    GeneWikii GTF2F1.
    GenomeRNAii 2962.
    NextBioi 11742.
    PMAP-CutDB P35269.
    PROi P35269.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi P35269.
    Bgeei P35269.
    CleanExi HS_GTF2F1.
    Genevestigatori P35269.

    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. "Characterization of cDNA for the large subunit of the transcription initiation factor TFIIF."
      Aso T., Vasavada H.A., Kawaguchi T., Germino F.J., Ganguly S., Kitajima S., Weissman S.M., Yasukochi Y.
      Nature 355:461-464(1992) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA], PARTIAL PROTEIN SEQUENCE.
    2. "A cDNA encoding RAP74, a general initiation factor for transcription by RNA polymerase II."
      Finkelstein A., Kostrub C.F., Li J., Chavez D.P., Wang B.Q., Fang S.M., Greenblatt J., Burton Z.F.
      Nature 355:464-467(1992) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA], PARTIAL PROTEIN SEQUENCE.
    3. "Cloning of human full-length CDSs in BD Creator(TM) system donor vector."
      Kalnine N., Chen X., Rolfs A., Halleck A., Hines L., Eisenstein S., Koundinya M., Raphael J., Moreira D., Kelley T., LaBaer J., Lin Y., Phelan M., Farmer A.
      Submitted (MAY-2003) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    4. "Complete sequencing and characterization of 21,243 full-length human cDNAs."
      Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.
      , Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.
      Nat. Genet. 36:40-45(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
      Tissue: Stomach.
    5. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    6. "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
      The MGC Project Team
      Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
      Tissue: Eye and Muscle.
    7. "Evolutionary conservation of human TATA-binding-polypeptide-associated factors TAFII31 and TAFII80 and interactions of TAFII80 with other TAFs and with general transcription factors."
      Hisatake K., Ohta T., Takada R., Guermah M., Horikoshi M., Nakatani Y., Roeder R.G.
      Proc. Natl. Acad. Sci. U.S.A. 92:8195-8199(1995) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH TAF6.
    8. "TAFII250 is a bipartite protein kinase that phosphorylates the base transcription factor RAP74."
      Dikstein R., Ruppert S., Tjian R.
      Cell 84:781-790(1996) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION AT SERINE RESIDUES.
    9. "Kinase activity and phosphorylation of the largest subunit of TFIIF transcription factor."
      Rossignol M., Keriel A., Staub A., Egly J.-M.
      J. Biol. Chem. 274:22387-22392(1999) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, PHOSPHORYLATION AT SER-385 AND THR-389, MUTAGENESIS OF SER-385 AND THR-389.
    10. "Interaction with general transcription factor IIF (TFIIF) is required for the suppression of activated transcription by RPB5-mediating protein (RMP)."
      Wei W., Gu J.X., Zhu C.Q., Sun F.Y., Dorjsuren D., Lin Y., Murakami S.
      Cell Res. 13:111-120(2003) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH URI1.
    11. "Global, in vivo, and site-specific phosphorylation dynamics in signaling networks."
      Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P., Mann M.
      Cell 127:635-648(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-217; SER-218; SER-221 AND SER-224, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    12. "Transcriptomic and proteomic analyses of rhabdomyosarcoma cells reveal differential cellular gene expression in response to enterovirus 71 infection."
      Leong W.F., Chow V.T.
      Cell. Microbiol. 8:565-580(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: INDUCTION, IDENTIFICATION BY MASS SPECTROMETRY.
    13. "A probability-based approach for high-throughput protein phosphorylation analysis and site localization."
      Beausoleil S.A., Villen J., Gerber S.A., Rush J., Gygi S.P.
      Nat. Biotechnol. 24:1285-1292(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-433, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    14. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-377; SER-380; SER-381; SER-385; THR-389; SER-431; SER-433; SER-436; THR-446 AND SER-449, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    15. "Lys-N and trypsin cover complementary parts of the phosphoproteome in a refined SCX-based approach."
      Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S.
      Anal. Chem. 81:4493-4501(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS], CLEAVAGE OF INITIATOR METHIONINE [LARGE SCALE ANALYSIS].
    16. "Quantitative phosphoproteomic analysis of T cell receptor signaling reveals system-wide modulation of protein-protein interactions."
      Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K., Rodionov V., Han D.K.
      Sci. Signal. 2:RA46-RA46(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-217; SER-218; SER-221; SER-224; SER-385 AND THR-389, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Leukemic T-cell.
    17. "Lysine acetylation targets protein complexes and co-regulates major cellular functions."
      Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T.C., Olsen J.V., Mann M.
      Science 325:834-840(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-407, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    18. "Quantitative phosphoproteomics reveals widespread full phosphorylation site occupancy during mitosis."
      Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L., Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M.
      Sci. Signal. 3:RA3-RA3(2010) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-217; SER-218; SER-221; SER-224 AND SER-433, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    19. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    20. "System-wide temporal characterization of the proteome and phosphoproteome of human embryonic stem cell differentiation."
      Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J., Johansen P.T., Kratchmarova I., Kassem M., Mann M., Olsen J.V., Blagoev B.
      Sci. Signal. 4:RS3-RS3(2011) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-217; SER-218; SER-224; THR-331; SER-385 AND SER-391, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    21. "Comparative large-scale characterisation of plant vs. mammal proteins reveals similar and idiosyncratic N-alpha acetylation features."
      Bienvenut W.V., Sumpton D., Martinez A., Lilla S., Espagne C., Meinnel T., Giglione C.
      Mol. Cell. Proteomics 11:M111.015131-M111.015131(2012) [PubMed] [Europe PMC] [Abstract]
      Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    22. Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    23. "Novel dimerization fold of RAP30/RAP74 in human TFIIF at 1.7 A resolution."
      Gaiser F., Tan S., Richmond T.J.
      J. Mol. Biol. 302:1119-1127(2000) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (1.7 ANGSTROMS) OF 5-153 IN COMPLEX WITH GTF2F2.
    24. "Crystal structure of the C-terminal domain of the RAP74 subunit of human transcription factor IIF."
      Kamada K., De Angelis J., Roeder R.G., Burley S.K.
      Proc. Natl. Acad. Sci. U.S.A. 98:3115-3120(2001) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (1.02 ANGSTROMS) OF 451-517.
    25. "Molecular mechanism of recruitment of TFIIF-associating RNA polymerase C-terminal domain phosphatase (FCP1) by transcription factor IIF."
      Kamada K., Roeder R.G., Burley S.K.
      Proc. Natl. Acad. Sci. U.S.A. 100:2296-2299(2003) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS) OF 449-517 IN COMPLEX WITH CTDP1.
    26. "Solution structure of the carboxyl-terminal domain of RAP74 and NMR characterization of the FCP1-binding sites of RAP74 and human TFIIB."
      Nguyen B.D., Chen H.T., Kobor M.S., Greenblatt J., Legault P., Omichinski J.G.
      Biochemistry 42:1460-1469(2003) [PubMed] [Europe PMC] [Abstract]
      Cited for: STRUCTURE BY NMR OF 451-517.
    27. "NMR structure of a complex containing the TFIIF subunit RAP74 and the RNA polymerase II carboxyl-terminal domain phosphatase FCP1."
      Nguyen B.D., Abbott K.L., Potempa K., Kobor M.S., Archambault J., Greenblatt J., Legault P., Omichinski J.G.
      Proc. Natl. Acad. Sci. U.S.A. 100:5688-5693(2003) [PubMed] [Europe PMC] [Abstract]
      Cited for: STRUCTURE BY NMR OF 451-517.

    Entry informationi

    Entry nameiT2FA_HUMAN
    AccessioniPrimary (citable) accession number: P35269
    Secondary accession number(s): B2RCS0, Q9BWN0
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: February 1, 1994
    Last sequence update: April 13, 2004
    Last modified: October 1, 2014
    This is version 153 of the entry and version 2 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programChordata Protein Annotation Program
    DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

    Miscellaneousi

    Caution

    Was reported to have a protein kinase activity and to autophosphorylates on Ser-385 and Thr-389.1 Publication

    Keywords - Technical termi

    3D-structure, Complete proteome, Direct protein sequencing, Reference proteome

    Documents

    1. Human chromosome 19
      Human chromosome 19: entries, gene names and cross-references to MIM
    2. Human entries with polymorphisms or disease mutations
      List of human entries with polymorphisms or disease mutations
    3. Human polymorphisms and disease mutations
      Index of human polymorphisms and disease mutations
    4. MIM cross-references
      Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
    5. PDB cross-references
      Index of Protein Data Bank (PDB) cross-references
    6. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3