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General transcription factor IIH, polypeptide 4, 52kDa
Identifiers
Symbols GTF2H4; TFIIH
External IDs OMIM601760 MGI1338799 HomoloGene7090 GeneCards: GTF2H4 Gene
RNA expression pattern
PBB GE GTF2H4 203577 at tn.png
More reference expression data
Orthologs
Species Human Mouse
Entrez 2968 14885
Ensembl ENSG00000137411 n/a
UniProt Q92759 n/a
RefSeq (mRNA) NM_001517 NM_010364
RefSeq (protein) NP_001508 NP_034494
Location (UCSC) Chr 6:
30.98 - 31 Mb
n/a
PubMed search [1] [2]

General transcription factor IIH subunit 4 is a protein that in humans is encoded by the GTF2H4 gene.[1][2]

Contents

Interactions

GTF2H4 has been shown to interact with MED21,[3] GTF2F1,[3] TATA binding protein,[3] XPB,[4][1] POLR2A[3] and Transcription Factor II B.[3]

See also

References

  1. ^ a b Marinoni JC, Roy R, Vermeulen W, Miniou P, Lutz Y, Weeda G, Seroz T, Gomez DM, Hoeijmakers JH, Egly JM (Apr 1997). "Cloning and characterization of p52, the fifth subunit of the core of the transcription/DNA repair factor TFIIH". EMBO J 16 (5): 1093–102. doi:10.1093/emboj/16.5.1093. PMID 9118947.  
  2. ^ "Entrez Gene: GTF2H4 general transcription factor IIH, polypeptide 4, 52kDa". http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=2968.  
  3. ^ a b c d e 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. (UNITED STATES) 94 (11): 5605–10. ISSN 0027-8424. PMID 9159119.  
  4. ^ Giglia-Mari, Giuseppina; Coin Frederic, Ranish Jeffrey A, Hoogstraten Deborah, Theil Arjan, Wijgers Nils, Jaspers Nicolaas G J, Raams Anja, Argentini Manuela, van der Spek P J, Botta Elena, Stefanini Miria, Egly Jean-Marc, Aebersold Ruedi, Hoeijmakers Jan H J, Vermeulen Wim (Jul. 2004). "A new, tenth subunit of TFIIH is responsible for the DNA repair syndrome trichothiodystrophy group A". Nat. Genet. (United States) 36 (7): 714–9. doi:10.1038/ng1387. ISSN 1061-4036. PMID 15226750.  

Further reading

  • Jeang KT (1998). "Tat, Tat-associated kinase, and transcription.". J. Biomed. Sci. 5 (1): 24–7. doi:10.1007/BF02253352. PMID 9570510.  
  • Yankulov K, Bentley D (1998). "Transcriptional control: Tat cofactors and transcriptional elongation.". Curr. Biol. 8 (13): R447–9. doi:10.1016/S0960-9822(98)70289-1. PMID 9651670.  
  • Maruyama K, Sugano S (1994). "Oligo-capping: a simple method to replace the cap structure of eukaryotic mRNAs with oligoribonucleotides.". Gene 138 (1-2): 171–4. doi:10.1016/0378-1119(94)90802-8. PMID 8125298.  
  • Blau J, Xiao H, McCracken S, et al. (1996). "Three functional classes of transcriptional activation domain.". Mol. Cell. Biol. 16 (5): 2044–55. PMID 8628270.  
  • Drapkin R, Le Roy G, Cho H, et al. (1996). "Human cyclin-dependent kinase-activating kinase exists in three distinct complexes.". Proc. Natl. Acad. Sci. U.S.A. 93 (13): 6488–93. doi:10.1073/pnas.93.13.6488. PMID 8692842.  
  • Zhou Q, Sharp PA (1996). "Tat-SF1: cofactor for stimulation of transcriptional elongation by HIV-1 Tat.". Science 274 (5287): 605–10. doi:10.1126/science.274.5287.605. PMID 8849451.  
  • Parada CA, Roeder RG (1996). "Enhanced processivity of RNA polymerase II triggered by Tat-induced phosphorylation of its carboxy-terminal domain.". Nature 384 (6607): 375–8. doi:10.1038/384375a0. PMID 8934526.  
  • García-Martínez LF, Ivanov D, Gaynor RB (1997). "Association of Tat with purified HIV-1 and HIV-2 transcription preinitiation complexes.". J. Biol. Chem. 272 (11): 6951–8. doi:10.1074/jbc.272.11.6951. PMID 9054383.  
  • Cujec TP, Cho H, Maldonado E, et al. (1997). "The human immunodeficiency virus transactivator Tat interacts with the RNA polymerase II holoenzyme.". Mol. Cell. Biol. 17 (4): 1817–23. PMID 9121429.  
  • Rossignol M, Kolb-Cheynel I, Egly JM (1997). "Substrate specificity of the cdk-activating kinase (CAK) is altered upon association with TFIIH.". Embo J. 16 (7): 1628–37. doi:10.1093/emboj/16.7.1628. PMID 9130708.  
  • Scully R, Anderson SF, Chao DM, et al. (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. PMID 9159119.  
  • García-Martínez LF, Mavankal G, Neveu JM, et al. (1997). "Purification of a Tat-associated kinase reveals a TFIIH complex that modulates HIV-1 transcription.". Embo J. 16 (10): 2836–50. doi:10.1093/emboj/16.10.2836. PMID 9184228.  
  • Nekhai S, Shukla RR, Kumar A (1997). "A human primary T-lymphocyte-derived human immunodeficiency virus type 1 Tat-associated kinase phosphorylates the C-terminal domain of RNA polymerase II and induces CAK activity.". J. Virol. 71 (10): 7436–41. PMID 9311822.  
  • Cujec TP, Okamoto H, Fujinaga K, et al. (1997). "The HIV transactivator TAT binds to the CDK-activating kinase and activates the phosphorylation of the carboxy-terminal domain of RNA polymerase II.". Genes Dev. 11 (20): 2645–57. doi:10.1101/gad.11.20.2645. PMID 9334327.  
  • Suzuki Y, Yoshitomo-Nakagawa K, Maruyama K, et al. (1997). "Construction and characterization of a full length-enriched and a 5'-end-enriched cDNA library.". Gene 200 (1-2): 149–56. doi:10.1016/S0378-1119(97)00411-3. PMID 9373149.  
  • Li XY, Green MR (1998). "The HIV-1 Tat cellular coactivator Tat-SF1 is a general transcription elongation factor.". Genes Dev. 12 (19): 2992–6. doi:10.1101/gad.12.19.2992. PMID 9765201.  
  • Ping YH, Rana TM (1999). "Tat-associated kinase (P-TEFb): a component of transcription preinitiation and elongation complexes.". J. Biol. Chem. 274 (11): 7399–404. doi:10.1074/jbc.274.11.7399. PMID 10066804.  

External links

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