AC T02188
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ID T02188
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DT 05.06.1997 (created); hiwi.
DT 07.03.2013 (updated); yre.
CO Copyright (C), QIAGEN.
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FA TFIIH-p34
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SY p34; p35.
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OS human, Homo sapiens
OC eukaryota; animalia; metazoa; chordata; vertebrata; tetrapoda; mammalia; eutheria; primates
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GE G006187 GTF2H3; HGNC: GTF2H3.
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SF part of TFIIH* subcomplex of TFIIH [2];
SF the potential zinc finger motif is involved in mediating DNA-binding by TFIIH [5];
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IN T02187 MAT1; human, Homo sapiens.
IN T02185 TFIIH-p44; human, Homo sapiens.
IN T02183 TFIIH-p62; human, Homo sapiens.
IN T02181 TFIIH-p90; human, Homo sapiens.
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DR TRANSPATH: MO000026213.
DR UniProtKB: Q13889;
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RN [1]; RE0005732.
RX PUBMED: 8152490.
RA Drapkin R., Reardon J. T., Ansari A., Huang J.-C., Zawel L., Ahn K., Sancar A., Reinberg D.
RT Dual role of TFIIH in DNA excision repair and in transcription by RNA polymerase II
RL Nature 368:769-772 (1994).
RN [2]; RE0005770.
RX PUBMED: 8692841.
RA Reardon J. T., Ge H., Gibbs E., Sancar A., Hurwitz J., Pan Z.-Q.
RT Isolation and characterization of two human transcription factor IIH(TFIIH)-related complexes: ERCC2/CAK and TFIIH*
RL Proc. Natl. Acad. Sci. USA 93:6482-6487 (1996).
RN [3]; RE0005773.
RX PUBMED: 1733973.
RA Flores O., Lu H., Reinberg D.
RT Factors involved in specific transcription by mammalian RNA polymerase II. Identification and characterization of factor IIH
RL J. Biol. Chem. 267:2786-2793 (1992).
RN [4]; RE0005775.
RX PUBMED: 1529339.
RA Fischer L., Gerard M., Chalut C., Lutz Y., Humbert S., Kanno M., Chambon P., Egly J.-M.
RT Cloning of the 62-kilodalton component of basic transcription factor BTF2
RL Science 257:1392-1395 (1992).
RN [5]; RE0005779.
RX PUBMED: 8194529.
RA Humbert S., van Vuuren H., Lutz Y., Hoeijmakers J. H. J., Egly J.-M., Moncollin V.
RT p44 and p34 subunits of the BTF2/TFIIH transcription factor have homologies with SSL1, a yeast protein involved in DNA repair
RL EMBO J. 13:2393-2398 (1994).
RN [6]; RE0023310.
RX PUBMED: 10748061.
RA Bastien J., Adam-Stitah S., Riedl T., Egly J. M., Chambon P., Rochette-Egly C.
RT TFIIH interacts with the retinoic acid receptor gamma and phosphorylates its AF-1-activating domain through cdk7.
RL J. Biol. Chem. 275:21896-21904 (2000).
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