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Gene Review

SUPT5H  -  suppressor of Ty 5 homolog (S. cerevisiae)

Homo sapiens

Synonyms: DRB sensitivity-inducing factor 160 kDa subunit, DRB sensitivity-inducing factor large subunit, DSIF large subunit, DSIF p160, FLJ34157, ...
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Disease relevance of SUPT5H


High impact information on SUPT5H

  • Consistent with capping enzyme binding, TFIIH-phosphorylated CTD stimulated guanylylation, and this increase was not additive with hSPT5 [3].
  • Methylation of SPT5 regulates its interaction with RNA polymerase II and transcriptional elongation properties [4].
  • Specific arginine residues in SPT5 that are methylated by these enzymes were identified and demonstrated to be important in regulating its promoter association and subsequent effects on transcriptional elongation [4].
  • These results suggest that methylation of SPT5 is an important posttranslational modification that is involved in regulating its transcriptional elongation properties in response to viral and cellular factors [4].
  • These data suggest that Spt4p, Spt5p, and, potentially, other regulators of Pol I transcription elongation play important roles in coupling rRNA transcription to its processing and ribosome assembly [5].

Chemical compound and disease context of SUPT5H

  • Flavopiridol, a potent P-TEFb kinase inhibitor, inhibits CTD phosphorylation, stable SPT5 binding, and histone methylation, suggesting that its potent antiviral activity is due to its ability to inhibit several critical and unique steps in HIV-1 transcription elongation [6].

Biological context of SUPT5H


Associations of SUPT5H with chemical compounds


Other interactions of SUPT5H


  1. Spt5 cooperates with human immunodeficiency virus type 1 Tat by preventing premature RNA release at terminator sequences. Bourgeois, C.F., Kim, Y.K., Churcher, M.J., West, M.J., Karn, J. Mol. Cell. Biol. (2002) [Pubmed]
  2. Domains in the SPT5 protein that modulate its transcriptional regulatory properties. Ivanov, D., Kwak, Y.T., Guo, J., Gaynor, R.B. Mol. Cell. Biol. (2000) [Pubmed]
  3. Transcription elongation factor hSPT5 stimulates mRNA capping. Wen, Y., Shatkin, A.J. Genes Dev. (1999) [Pubmed]
  4. Methylation of SPT5 regulates its interaction with RNA polymerase II and transcriptional elongation properties. Kwak, Y.T., Guo, J., Prajapati, S., Park, K.J., Surabhi, R.M., Miller, B., Gehrig, P., Gaynor, R.B. Mol. Cell (2003) [Pubmed]
  5. RNA polymerase II elongation factors Spt4p and Spt5p play roles in transcription elongation by RNA polymerase I and rRNA processing. Schneider, D.A., French, S.L., Osheim, Y.N., Bailey, A.O., Vu, L., Dodd, J., Yates, J.R., Beyer, A.L., Nomura, M. Proc. Natl. Acad. Sci. U.S.A. (2006) [Pubmed]
  6. Coordination of transcription factor phosphorylation and histone methylation by the P-TEFb kinase during human immunodeficiency virus type 1 transcription. Zhou, M., Deng, L., Lacoste, V., Park, H.U., Pumfery, A., Kashanchi, F., Brady, J.N., Kumar, A. J. Virol. (2004) [Pubmed]
  7. Modulating HIV-1 replication by RNA interference directed against human transcription elongation factor SPT5. Ping, Y.H., Chu, C.Y., Cao, H., Jacque, J.M., Stevenson, M., Rana, T.M. Retrovirology (2004) [Pubmed]
  8. Positive transcription elongation factor B phosphorylates hSPT5 and RNA polymerase II carboxyl-terminal domain independently of cyclin-dependent kinase-activating kinase. Kim, J.B., Sharp, P.A. J. Biol. Chem. (2001) [Pubmed]
  9. Isolation, sequencing, and mapping of the human homologue of the yeast transcription factor, SPT5. Chiang, P.W., Fogel, E., Jackson, C.L., Lieuallen, K., Lennon, G., Qu, X., Wang, S.Q., Kurnit, D.M. Genomics (1996) [Pubmed]
  10. Control of eukaryotic transcription elongation. Winston, F. Genome Biol. (2001) [Pubmed]
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