GTF2F1

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General transcription factor IIF, polypeptide 1, 74kDa

PDB rendering based on 1f3u.
Available structures
PDB Ortholog search: PDBe, RCSB
Identifiers
Symbols GTF2F1 ; BTF4; RAP74; TF2F1; TFIIF
External IDs OMIM189968 MGI1923848 HomoloGene1585 GeneCards: GTF2F1 Gene
Orthologs
Species Human Mouse
Entrez 2962 98053
Ensembl ENSG00000125651 ENSMUSG00000002658
UniProt P35269 Q3THK3
RefSeq (mRNA) NM_002096 NM_133801
RefSeq (protein) NP_002087 NP_598562
Location (UCSC) Chr 19:
6.38 – 6.39 Mb
Chr 17:
57 – 57.01 Mb
PubMed search [1] [2]

General transcription factor IIF subunit 1 is a protein that in humans is encoded by the GTF2F1 gene.[1][2]

Interactions[edit]

GTF2F1 has been shown to interact with TAF1,[3][4][5][6] HNRPU,[7] GTF2H4,[8] CTDP1,[9] TATA binding protein,[4][6][8] POLR2A,[8][10] MED21,[8][11] TAF11,[8] Serum response factor[12][13] and Transcription Factor II B.[8][14]

See also[edit]

References[edit]

  1. ^ Finkelstein A, Kostrub CF, Li J, Chavez DP, Wang BQ, Fang SM, Greenblatt J, Burton ZF (March 1992). "A cDNA encoding RAP74, a general initiation factor for transcription by RNA polymerase II". Nature 355 (6359): 464–7. doi:10.1038/355464a0. PMID 1734284. 
  2. ^ "Entrez Gene: GTF2F1 general transcription factor IIF, polypeptide 1, 74kDa". 
  3. ^ Dikstein R, Ruppert S, Tjian R (March 1996). "TAFII250 is a bipartite protein kinase that phosphorylates the base transcription factor RAP74". Cell 84 (5): 781–90. doi:10.1016/S0092-8674(00)81055-7. PMID 8625415. 
  4. ^ a b Ruppert S, Tjian R (November 1995). "Human TAFII250 interacts with RAP74: implications for RNA polymerase II initiation". Genes Dev. 9 (22): 2747–55. doi:10.1101/gad.9.22.2747. PMID 7590250. 
  5. ^ Siegert JL, Robbins P D (January 1999). "Rb inhibits the intrinsic kinase activity of TATA-binding protein-associated factor TAFII250". Mol. Cell. Biol. 19 (1): 846–54. PMC 83941. PMID 9858607. 
  6. ^ a b Malik S, Guermah M, Roeder R G (March 1998). "A dynamic model for PC4 coactivator function in RNA polymerase II transcription". Proc Natl Acad Sci U S A 95 (5): 2192–7. doi:10.1073/pnas.95.5.2192. PMC 19292. PMID 9482861. 
  7. ^ Kim MK, Nikodem V M (October 1999). "hnRNP U inhibits carboxy-terminal domain phosphorylation by TFIIH and represses RNA polymerase II elongation". Mol. Cell. Biol. 19 (10): 6833–44. PMC 84680. PMID 10490622. 
  8. ^ a b c d e f Scully R, Anderson S F, Chao D M, Wei W, Ye L, Young R A, Livingston D M, Parvin J D (May 1997). "BRCA1 is a component of the RNA polymerase II holoenzyme". Proc Natl Acad Sci U S A 94 (11): 5605–10. doi:10.1073/pnas.94.11.5605. PMC 20825. PMID 9159119. 
  9. ^ Archambault J, Pan G, Dahmus G K, Cartier M, Marshall N, Zhang S, Dahmus M E, Greenblatt J (October 1998). "FCP1, the RAP74-interacting subunit of a human protein phosphatase that dephosphorylates the carboxyl-terminal domain of RNA polymerase IIO". J. Biol. Chem. 273 (42): 27593–601. doi:10.1074/jbc.273.42.27593. PMID 9765293. 
  10. ^ Cho H, Orphanides G, Sun X, Yang X J, Ogryzko V, Lees E, Nakatani Y, Reinberg D (September 1998). "A human RNA polymerase II complex containing factors that modify chromatin structure". Mol. Cell. Biol. 18 (9): 5355–63. PMC 109120. PMID 9710619. 
  11. ^ Suñé C, Hayashi T, Liu Y, Lane W S, Young R A, Garcia-Blanco M A (October 1997). "CA150, a nuclear protein associated with the RNA polymerase II holoenzyme, is involved in Tat-activated human immunodeficiency virus type 1 transcription". Mol. Cell. Biol. 17 (10): 6029–39. PMC 232452. PMID 9315662. 
  12. ^ Joliot V, Demma M, Prywes R (February 1995). "Interaction with RAP74 subunit of TFIIF is required for transcriptional activation by serum response factor". Nature 373 (6515): 632–5. doi:10.1038/373632a0. PMID 7854423. 
  13. ^ Zhu H, Joliot V, Prywes R (February 1994). "Role of transcription factor TFIIF in serum response factor-activated transcription". J. Biol. Chem. 269 (5): 3489–97. PMID 8106390. 
  14. ^ Fang SM, Burton Z F (May 1996). "RNA polymerase II-associated protein (RAP) 74 binds transcription factor (TF) IIB and blocks TFIIB-RAP30 binding". J. Biol. Chem. 271 (20): 11703–9. doi:10.1074/jbc.271.20.11703. PMID 8662660. 

Further reading[edit]

External links[edit]

This article incorporates text from the United States National Library of Medicine, which is in the public domain.