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SUPT16H
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<h2 id="function">Function</h2> <p>Transcription of protein-coding genes can be reconstituted on naked DNA with only the <a href="/facts/General_transcription_factor/Vuh1hhLy">general transcription factors</a> and <a href="/facts/RNA_polymerase_II/MK2kgybw">RNA polymerase II</a>. However, this minimal system cannot transcribe DNA packaged into <a href="/facts/Chromatin/ha0TJheJ">chromatin</a>, indicating that accessory factors may facilitate access to DNA. One such factor, <a href="/facts/FACT_(biology)/TC1khKg2">FACT</a> (facilitates chromatin transcription), interacts specifically with histones <a href="/facts/Histone_H2A/mE8C347j">H2A</a>/<a href="/facts/Histone_H2B/h8gyE0fp">H2B</a> to effect <a href="/facts/Nucleosome/HX5DR9bn">nucleosome</a> disassembly and transcription elongation. FACT is composed of an 80 kDa subunit and a 140 kDa subunit, the latter of which is the protein encoded by this gene.<a class="footnote-ref" id="fnref:4" href="#fn:4"><sup>4</sup></a> </p> <h2 id="further-reading">Further reading</h2> <ul><li>LeRoy G, Orphanides G, Lane WS, Reinberg D (1998). "Requirement of RSF and FACT for transcription of chromatin templates in vitro". <i>Science</i>. 282 (5395): 1900–4. <a href="/facts/Doi_(identifier)/muM9Etpq">doi</a>:<a href="https://doi.org/10.1126%2Fscience.282.5395.1900">10.1126/science.282.5395.1900</a>. <a href="/facts/PMID_(identifier)/JlHAvMHt">PMID</a> <a href="https://pubmed.ncbi.nlm.nih.gov/9836642">9836642</a>.</li> <li>Orphanides G, Wu WH, Lane WS, Hampsey M, Reinberg D (1999). "The chromatin-specific transcription elongation factor FACT comprises human SPT16 and SSRP1 proteins". <i>Nature</i>. 400 (6741): 284–8. <a href="/facts/Bibcode_(identifier)/9HtdQSGB">Bibcode</a>:<a href="https://ui.adsabs.harvard.edu/abs/1999Natur.400..284O">1999Natur.400..284O</a>. <a href="/facts/Doi_(identifier)/muM9Etpq">doi</a>:<a href="https://doi.org/10.1038%2F22350">10.1038/22350</a>. <a href="/facts/PMID_(identifier)/JlHAvMHt">PMID</a> <a href="https://pubmed.ncbi.nlm.nih.gov/10421373">10421373</a>. <a href="/facts/S2CID_(identifier)/ldJsHa2Y">S2CID</a> <a href="https://api.semanticscholar.org/CorpusID:4300397">4300397</a>.</li> <li>Kang SW, Kuzuhara T, Horikoshi M (2000). "Functional interaction of general transcription initiation factor TFIIE with general chromatin factor SPT16/CDC68". <i>Genes Cells</i>. 5 (4): 251–63. <a href="/facts/Doi_(identifier)/muM9Etpq">doi</a>:<a href="https://doi.org/10.1046%2Fj.1365-2443.2000.00323.x">10.1046/j.1365-2443.2000.00323.x</a>. <a href="/facts/PMID_(identifier)/JlHAvMHt">PMID</a> <a href="https://pubmed.ncbi.nlm.nih.gov/10792464">10792464</a>. <a href="/facts/S2CID_(identifier)/ldJsHa2Y">S2CID</a> <a href="https://api.semanticscholar.org/CorpusID:33454256">33454256</a>.</li> <li>Wada T, Orphanides G, Hasegawa J, Kim DK, Shima D, Yamaguchi Y, Fukuda A, Hisatake K, Oh S, Reinberg D, Handa H (2000). <a href="https://doi.org/10.1016%2FS1097-2765%2800%2980272-5">"FACT relieves DSIF/NELF-mediated inhibition of transcriptional elongation and reveals functional differences between P-TEFb and TFIIH"</a>. <i>Mol. Cell</i>. 5 (6): 1067–72. <a href="/facts/Doi_(identifier)/muM9Etpq">doi</a>:<a href="https://doi.org/10.1016%2FS1097-2765%2800%2980272-5">10.1016/S1097-2765(00)80272-5</a>. <a href="/facts/PMID_(identifier)/JlHAvMHt">PMID</a> <a href="https://pubmed.ncbi.nlm.nih.gov/10912001">10912001</a>.</li> <li>Keller DM, Lu H (2003). <a href="https://doi.org/10.1074%2Fjbc.M209820200">"p53 serine 392 phosphorylation increases after UV through induction of the assembly of the CK2.hSPT16.SSRP1 complex"</a>. <i>J. Biol. Chem</i>. 277 (51): 50206–13. <a href="/facts/Doi_(identifier)/muM9Etpq">doi</a>:<a href="https://doi.org/10.1074%2Fjbc.M209820200">10.1074/jbc.M209820200</a>. <a href="/facts/PMID_(identifier)/JlHAvMHt">PMID</a> <a href="https://pubmed.ncbi.nlm.nih.gov/12393879">12393879</a>.</li> <li>Belotserkovskaya R, Oh S, Bondarenko VA, Orphanides G, Studitsky VM, Reinberg D (2003). "FACT facilitates transcription-dependent nucleosome alteration". <i>Science</i>. 301 (5636): 1090–3. <a href="/facts/Bibcode_(identifier)/9HtdQSGB">Bibcode</a>:<a href="https://ui.adsabs.harvard.edu/abs/2003Sci...301.1090B">2003Sci...301.1090B</a>. <a href="/facts/Doi_(identifier)/muM9Etpq">doi</a>:<a href="https://doi.org/10.1126%2Fscience.1085703">10.1126/science.1085703</a>. <a href="/facts/PMID_(identifier)/JlHAvMHt">PMID</a> <a href="https://pubmed.ncbi.nlm.nih.gov/12934006">12934006</a>. <a href="/facts/S2CID_(identifier)/ldJsHa2Y">S2CID</a> <a href="https://api.semanticscholar.org/CorpusID:26667338">26667338</a>.</li> <li>Li J, Hawkins IC, Harvey CD, Jennings JL, Link AJ, Patton JG (2003). <a href="https://www.ncbi.nlm.nih.gov/pmc/articles/PMC207616">"Regulation of Alternative Splicing by SRrp86 and Its Interacting Proteins"</a>. <i>Mol. Cell. Biol</i>. 23 (21): 7437–47. <a href="/facts/Doi_(identifier)/muM9Etpq">doi</a>:<a href="https://doi.org/10.1128%2FMCB.23.21.7437-7447.2003">10.1128/MCB.23.21.7437-7447.2003</a>. <a href="/facts/PMC_(identifier)/dX1zMt71">PMC</a> <a href="https://www.ncbi.nlm.nih.gov/pmc/articles/PMC207616">207616</a>. <a href="/facts/PMID_(identifier)/JlHAvMHt">PMID</a> <a href="https://pubmed.ncbi.nlm.nih.gov/14559993">14559993</a>.</li> <li>Tan BC, Lee SC (2004). <a href="https://doi.org/10.1074%2Fjbc.M311477200">"Nek9, a novel FACT-associated protein, modulates interphase progression"</a>. <i>J. Biol. Chem</i>. 279 (10): 9321–30. <a href="/facts/Doi_(identifier)/muM9Etpq">doi</a>:<a href="https://doi.org/10.1074%2Fjbc.M311477200">10.1074/jbc.M311477200</a>. <a href="/facts/PMID_(identifier)/JlHAvMHt">PMID</a> <a href="https://pubmed.ncbi.nlm.nih.gov/14660563">14660563</a>.</li> <li>Fryer CJ, White JB, Jones KA (2005). <a href="https://doi.org/10.1016%2Fj.molcel.2004.10.014">"Mastermind recruits CycC:CDK8 to phosphorylate the Notch ICD and coordinate activation with turnover"</a>. <i>Mol. Cell</i>. 16 (4): 509–20. <a href="/facts/Doi_(identifier)/muM9Etpq">doi</a>:<a href="https://doi.org/10.1016%2Fj.molcel.2004.10.014">10.1016/j.molcel.2004.10.014</a>. <a href="/facts/PMID_(identifier)/JlHAvMHt">PMID</a> <a href="https://pubmed.ncbi.nlm.nih.gov/15546612">15546612</a>.</li> <li>Kouskouti A, Talianidis I (2005). <a href="https://www.ncbi.nlm.nih.gov/pmc/articles/PMC545808">"Histone modifications defining active genes persist after transcriptional and mitotic inactivation"</a>. <i>EMBO J</i>. 24 (2): 347–57. <a href="/facts/Doi_(identifier)/muM9Etpq">doi</a>:<a href="https://doi.org/10.1038%2Fsj.emboj.7600516">10.1038/sj.emboj.7600516</a>. <a href="/facts/PMC_(identifier)/dX1zMt71">PMC</a> <a href="https://www.ncbi.nlm.nih.gov/pmc/articles/PMC545808">545808</a>. <a href="/facts/PMID_(identifier)/JlHAvMHt">PMID</a> <a href="https://pubmed.ncbi.nlm.nih.gov/15616580">15616580</a>.</li> <li>Huang JY, Chen WH, Chang YL, Wang HT, Chuang WT, Lee SC (2006). <a href="https://www.ncbi.nlm.nih.gov/pmc/articles/PMC1458519">"Modulation of nucleosome-binding activity of FACT by poly(ADP-ribosyl)ation"</a>. <i>Nucleic Acids Res</i>. 34 (8): 2398–407. <a href="/facts/Doi_(identifier)/muM9Etpq">doi</a>:<a href="https://doi.org/10.1093%2Fnar%2Fgkl241">10.1093/nar/gkl241</a>. <a href="/facts/PMC_(identifier)/dX1zMt71">PMC</a> <a href="https://www.ncbi.nlm.nih.gov/pmc/articles/PMC1458519">1458519</a>. <a href="/facts/PMID_(identifier)/JlHAvMHt">PMID</a> <a href="https://pubmed.ncbi.nlm.nih.gov/16682447">16682447</a>.</li> <li>Pavri R, Zhu B, Li G, Trojer P, Mandal S, Shilatifard A, Reinberg D (2006). <a href="https://doi.org/10.1016%2Fj.cell.2006.04.029">"Histone H2B monoubiquitination functions cooperatively with FACT to regulate elongation by RNA polymerase II"</a>. <i>Cell</i>. 125 (4): 703–17. <a href="/facts/Doi_(identifier)/muM9Etpq">doi</a>:<a href="https://doi.org/10.1016%2Fj.cell.2006.04.029">10.1016/j.cell.2006.04.029</a>. <a href="/facts/PMID_(identifier)/JlHAvMHt">PMID</a> <a href="https://pubmed.ncbi.nlm.nih.gov/16713563">16713563</a>.</li> <li>Tan BC, Chien CT, Hirose S, Lee SC (2006). <a href="https://www.ncbi.nlm.nih.gov/pmc/articles/PMC1560368">"Functional cooperation between FACT and MCM helicase facilitates initiation of chromatin DNA replication"</a>. <i>EMBO J</i>. 25 (17): 3975–85. <a href="/facts/Doi_(identifier)/muM9Etpq">doi</a>:<a href="https://doi.org/10.1038%2Fsj.emboj.7601271">10.1038/sj.emboj.7601271</a>. <a href="/facts/PMC_(identifier)/dX1zMt71">PMC</a> <a href="https://www.ncbi.nlm.nih.gov/pmc/articles/PMC1560368">1560368</a>. <a href="/facts/PMID_(identifier)/JlHAvMHt">PMID</a> <a href="https://pubmed.ncbi.nlm.nih.gov/16902406">16902406</a>.</li> <li>Biswas D, Dutta-Biswas R, Mitra D, Shibata Y, Strahl BD, Formosa T, Stillman DJ (2006). <a href="https://www.ncbi.nlm.nih.gov/pmc/articles/PMC1589996">"Opposing roles for Set2 and yFACT in regulating TBP binding at promoters"</a>. <i>EMBO J</i>. 25 (19): 4479–89. <a href="/facts/Doi_(identifier)/muM9Etpq">doi</a>:<a href="https://doi.org/10.1038%2Fsj.emboj.7601333">10.1038/sj.emboj.7601333</a>. <a href="/facts/PMC_(identifier)/dX1zMt71">PMC</a> <a href="https://www.ncbi.nlm.nih.gov/pmc/articles/PMC1589996">1589996</a>. <a href="/facts/PMID_(identifier)/JlHAvMHt">PMID</a> <a href="https://pubmed.ncbi.nlm.nih.gov/16977311">16977311</a>.</li></ul> <h2 id="external-links">External links</h2> <ul><li>Overview of all the structural information available in the <a href="/facts/Protein_Data_Bank/oUhq4ABD">PDB</a> for <a href="/facts/UniProt/lfDDHjAl">UniProt</a>: <i><a href="https://www.ebi.ac.uk/pdbe/pdbe-kb/proteins/Q9Y5B9">Q9Y5B9</a></i> (FACT complex subunit SPT16) at the <a href="/facts/PDBe-KB/p1WX7lPH">PDBe-KB</a>.</li></ul> <h2 id="references">References</h2> <ol> <li id="fn:1"><p>Orphanides G, LeRoy G, Chang CH, Luse DS, Reinberg D (Mar 1998). "FACT, a factor that facilitates transcript elongation through nucleosomes". Cell. 92 (1): 105–16. doi:10.1016/S0092-8674(00)80903-4. PMID 9489704. <a href="https://doi.org/10.1016%2FS0092-8674%2800%2980903-4" target="_blank">https://doi.org/10.1016%2FS0092-8674%2800%2980903-4</a> <a href="#fnref:1" class="footnote-back-ref">↩</a></p></li> <li id="fn:2"><p>Keller DM, Zeng X, Wang Y, Zhang QH, Kapoor M, Shu H, Goodman R, Lozano G, Zhao Y, Lu H (Mar 2001). "A DNA damage-induced p53 serine 392 kinase complex contains CK2, hSpt16, and SSRP1". Mol Cell. 7 (2): 283–92. doi:10.1016/S1097-2765(01)00176-9. PMID 11239457. <a href="https://doi.org/10.1016%2FS1097-2765%2801%2900176-9" target="_blank">https://doi.org/10.1016%2FS1097-2765%2801%2900176-9</a> <a href="#fnref:2" class="footnote-back-ref">↩</a></p></li> <li id="fn:3"><p>"Entrez Gene: SUPT16H suppressor of Ty 16 homolog (S. cerevisiae)". <a href="https://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=11198" target="_blank">https://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=11198</a> <a href="#fnref:3" class="footnote-back-ref">↩</a></p></li> <li id="fn:4"><p>"Entrez Gene: SUPT16H suppressor of Ty 16 homolog (S. cerevisiae)". <a href="https://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=11198" target="_blank">https://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=11198</a> <a href="#fnref:4" class="footnote-back-ref">↩</a></p></li> </ol>