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GTF2H1: Wikis


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From Wikipedia, the free encyclopedia

General transcription factor IIH, polypeptide 1, 62kDa

PDB rendering based on 1pfj.
Available structures
1pfj, 2dii
Symbols GTF2H1; BTF2; TFIIH
External IDs OMIM189972 MGI1277216 HomoloGene3885 GeneCards: GTF2H1 Gene
RNA expression pattern
PBB GE GTF2H1 202451 at tn.png
PBB GE GTF2H1 202453 s at tn.png
More reference expression data
Species Human Mouse
Entrez 2965 14884
Ensembl ENSG00000110768 ENSMUSG00000006599
UniProt P32780 Q7TPY0
RefSeq (mRNA) NM_005316 NM_008186
RefSeq (protein) NP_005307 NP_032212
Location (UCSC) Chr 11:
18.3 - 18.35 Mb
Chr 7:
46.66 - 46.69 Mb
PubMed search [1] [2]

General transcription factor IIH subunit 1 is a protein that in humans is encoded by the GTF2H1 gene.[1][2][3]



GTF2H1 has been shown to interact with E2F1,[4] XPB,[5][6][7] ERCC2,[8][7] Estrogen receptor alpha,[9] Cyclin-dependent kinase 7[7][10][11] and TCEA1.[12][13]

See also


  1. ^ Fischer L, Gerard M, Chalut C, Lutz Y, Humbert S, Kanno M, Chambon P, Egly JM (Oct 1992). "Cloning of the 62-kilodalton component of basic transcription factor BTF2". Science 257 (5075): 1392–5. PMID 1529339.  
  2. ^ Heng HH, Xiao H, Shi XM, Greenblatt J, Tsui LC (May 1994). "Genes encoding general initiation factors for RNA polymerase II transcription are dispersed in the human genome". Hum Mol Genet 3 (1): 61–4. PMID 8162052.  
  3. ^ "Entrez Gene: GTF2H1 general transcription factor IIH, polypeptide 1, 62kDa".  
  4. ^ Vandel, L; Kouzarides T (Aug. 1999). "Residues phosphorylated by TFIIH are required for E2F-1 degradation during S-phase". EMBO J. (ENGLAND) 18 (15): 4280–91. doi:10.1093/emboj/18.15.4280. ISSN 0261-4189. PMID 10428966.  
  5. ^ 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.  
  6. ^ Marinoni, J C; Roy R, Vermeulen W, Miniou P, Lutz Y, Weeda G, Seroz T, Gomez D M, Hoeijmakers J H, Egly J M (Mar. 1997). "Cloning and characterization of p52, the fifth subunit of the core of the transcription/DNA repair factor TFIIH". EMBO J. (ENGLAND) 16 (5): 1093–102. doi:10.1093/emboj/16.5.1093. ISSN 0261-4189. PMID 9118947.  
  7. ^ a b c Rossignol, M; Kolb-Cheynel I, Egly J M (Apr. 1997). "Substrate specificity of the cdk-activating kinase (CAK) is altered upon association with TFIIH". EMBO J. (ENGLAND) 16 (7): 1628–37. doi:10.1093/emboj/16.7.1628. ISSN 0261-4189. PMID 9130708.  
  8. ^ Drapkin, R; Reardon J T, Ansari A, Huang J C, Zawel L, Ahn K, Sancar A, Reinberg D (Apr. 1994). "Dual role of TFIIH in DNA excision repair and in transcription by RNA polymerase II". Nature (ENGLAND) 368 (6473): 769–72. doi:10.1038/368769a0. ISSN 0028-0836. PMID 8152490.  
  9. ^ Chen, D; Riedl T, Washbrook E, Pace P E, Coombes R C, Egly J M, Ali S (Jul. 2000). "Activation of estrogen receptor alpha by S118 phosphorylation involves a ligand-dependent interaction with TFIIH and participation of CDK7". Mol. Cell (UNITED STATES) 6 (1): 127–37. ISSN 1097-2765. PMID 10949034.  
  10. ^ Shiekhattar, R; Mermelstein F, Fisher R P, Drapkin R, Dynlacht B, Wessling H C, Morgan D O, Reinberg D (Mar. 1995). "Cdk-activating kinase complex is a component of human transcription factor TFIIH". Nature (ENGLAND) 374 (6519): 283–7. doi:10.1038/374283a0. ISSN 0028-0836. PMID 7533895.  
  11. ^ Yee, A; Nichols M A, Wu L, Hall F L, Kobayashi R, Xiong Y (Dec. 1995). "Molecular cloning of CDK7-associated human MAT1, a cyclin-dependent kinase-activating kinase (CAK) assembly factor". Cancer Res. (UNITED STATES) 55 (24): 6058–62. ISSN 0008-5472. PMID 8521393.  
  12. ^ Archambault, J; Pan G, Dahmus G K, Cartier M, Marshall N, Zhang S, Dahmus M E, Greenblatt J (Oct. 1998). "FCP1, the RAP74-interacting subunit of a human protein phosphatase that dephosphorylates the carboxyl-terminal domain of RNA polymerase IIO". J. Biol. Chem. (UNITED STATES) 273 (42): 27593–601. ISSN 0021-9258. PMID 9765293.  
  13. ^ Pan, G; Aso T, Greenblatt J (Sep. 1997). "Interaction of elongation factors TFIIS and elongin A with a human RNA polymerase II holoenzyme capable of promoter-specific initiation and responsive to transcriptional activators". J. Biol. Chem. (UNITED STATES) 272 (39): 24563–71. ISSN 0021-9258. PMID 9305922.  

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.  
  • Shiekhattar R, Mermelstein F, Fisher RP, et al. (1995). "Cdk-activating kinase complex is a component of human transcription factor TFIIH.". Nature 374 (6519): 283–7. doi:10.1038/374283a0. PMID 7533895.  
  • Tong X, Drapkin R, Reinberg D, Kieff E (1995). "The 62- and 80-kDa subunits of transcription factor IIH mediate the interaction with Epstein-Barr virus nuclear protein 2.". Proc. Natl. Acad. Sci. U.S.A. 92 (8): 3259–63. doi:10.1073/pnas.92.8.3259. PMID 7724549.  
  • Fantes JA, Oghene K, Boyle S, et al. (1995). "A high-resolution integrated physical, cytogenetic, and genetic map of human chromosome 11: distal p13 to proximal p15.1.". Genomics 25 (2): 447–61. doi:10.1016/0888-7543(95)80045-N. PMID 7789978.  
  • Xiao H, Pearson A, Coulombe B, et al. (1994). "Binding of basal transcription factor TFIIH to the acidic activation domains of VP16 and p53.". Mol. Cell. Biol. 14 (10): 7013–24. PMID 7935417.  
  • Schaeffer L, Moncollin V, Roy R, et al. (1994). "The ERCC2/DNA repair protein is associated with the class II BTF2/TFIIH transcription factor.". Embo J. 13 (10): 2388–92. PMID 8194528.  
  • 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.  
  • Iyer N, Reagan MS, Wu KJ, et al. (1996). "Interactions involving the human RNA polymerase II transcription/nucleotide excision repair complex TFIIH, the nucleotide excision repair protein XPG, and Cockayne syndrome group B (CSB) protein.". Biochemistry 35 (7): 2157–67. doi:10.1021/bi9524124. PMID 8652557.  
  • Reardon JT, Ge H, Gibbs E, et al. (1996). "Isolation and characterization of two human transcription factor IIH (TFIIH)-related complexes: ERCC2/CAK and TFIIH.". Proc. Natl. Acad. Sci. U.S.A. 93 (13): 6482–7. doi:10.1073/pnas.93.13.6482. PMID 8692841.  
  • 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.  
  • Marinoni JC, Roy R, Vermeulen W, et al. (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.  
  • 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.  
  • 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.  

External links

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



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